Przewidywanie ciężkości COVID-19 za pomocą swoistego przeciwciała nukleokapsydowego i wskaźnika czynnika ryzyka choroby
Steidzami nepieciešamas efektīvas metodes COVID-19 slimības trajektoriju prognozēšanai. Šeit ar enzīmu saistītu imūnsorbentu testu (ELISA) un koronavīrusa antigēna mikroelementu (COVAM) analīze uzrādīja antivielu epitopus COVID-19 pacientu (n = 86) plazmā, kuriem bija plašs slimību stāvoklis. Eksperimentos tika identificētas antivielas pret 21 atlikuma epitopu no nukleokapsīda (saukts par Ep9), kas saistīts ar smagu slimību, ieskaitot uzņemšanu intensīvās terapijas nodaļā (ICU), nepieciešamību pēc ventilatoriem vai nāvi.
Svarīgi, ka anti-Ep9 antivielas var noteikt 6 dienu laikā pēc simptomu parādīšanās un dažreiz 1 dienas laikā. Turklāt anti-Ep9 antivielas korelē ar dažādām blakusslimībām un imūnās hiperaktivitātes pazīmēm. Mēs ieviešam vienkārši aprēķināmu slimības riska faktora rādītāju, lai aprēķinātu katra pacienta blakusslimības un vecumu. Pacientiem ar anti-Ep9 antivielām rādītāji virs 3,Zero paredz smagākus slimības iznākumus ar 13,42 varbūtības koeficientu (96,7% specifiskumu).
Rezultāti ir pamats jauna veida COVID-19 prognostikai, lai ļautu agri identificēt un šķirot augsta riska pacientus. Šāda informācija varētu palīdzēt efektīvākai terapeitiskai iejaukšanai. SVARĪBA COVID-19 pandēmija ir izraisījusi vairāk nekā divus miljonus nāves gadījumu visā pasaulē. Neskatoties uz centieniem cīnīties ar vīrusu, šī slimība joprojām pārņem slimnīcas ar smagi slimiem pacientiem.
COVID-19 diagnostiku var viegli veikt, izmantojot daudzas uzticamas testēšanas platformas; tomēr prognostiskā prognozēšana joprojām ir nenotverama. Šajā nolūkā mēs identificējām īsu epitopu no SARS-CoV-2 nukleokapsīda proteīna, kā arī slimības riska faktora rādītāju, pamatojoties uz blakusslimībām un vecumu. Antivielu klātbūtne, kas specifiski saistās ar šo epitopu, kā arī vērtējuma robežvērtība var paredzēt smagus COVID-19 rezultātus ar 96,7% specifiskumu.
Związek między poziomami alarmin w surowicy a wskaźnikami specyficznymi dla choroby u pacjentów z zapaleniem naczyń związanym z cytoplazmatycznymi przeciwciałami przeciw neutrofilom
Priekšvēsture / mērķis: Mēs novērtējām sakarību starp seruma alarmīna līmeni un slimības specifiskajiem rādītājiem pacientiem ar anti-neitrofilo citoplazmas antivielu (ANCA) saistīto vaskulītu (AAV).
Pacienti un metodes: Tika izmantoti serumi un dati par 79 pacientiem. AAV specifiskajiem indeksiem tika savākts Birmingemas vaskulīta aktivitātes rādītājs (BVAS), piecu faktoru rādītājs (FFS) un vaskulīta bojājuma indekss (VDI), kā arī četru alarmīnu līmenis (hepatomas atvasināts augšanas faktors, augstas mobilitātes grupas 1. proteīns) , S100A9 un S100A12) tika mērīti, izmantojot ar enzīmu saistītu imūnsorbentu testu. Tika novērtētas asociācijas starp alarminu līmeni, AAV specifiskajiem indeksiem un iekaisuma laboratorijas marķieriem.
Rezultāti: S100A9 līmenis būtiski korelēja ar C-reaktīvo olbaltumvielu līmeni (r = 0,316, p = 0,005) un S100A12 līmenis korelēja ar VDI (r = 0,232, p = 0,040), kas bija konsekventa pacientu apakšgrupā ar mieloperoksidāzi (perinukleārā) ) -ANCA pozitivitāte. Citas asociācijas starp alarminu līmeni un BVAS, FFS un VDI netika atrastas.
Secinājums: seruma S100A12 līmenis bija saistīts ar orgānu bojājumiem AAV, īpaši mieloperoksidāzes (perinukleārās) -ANCA pozitīviem pacientiem.
Description: IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP4 is the major IGF-BP produced by osteoblasts, and is also found in the epidermis, ovarian follicles, and other tissues. IGF-BP4 inhibits the activity of IGF-I and IGF-II by binding in a manner that results in the formation of complexes with reduced ability to signal through cell surface IGF receptors. IGF-BP4 can inhibit the growth of chick pelvis cartilage and HT29 colon adenocarcinoma cells by blocking the mitogenic actions of IGFs, and has also been shown to reduce colony formation by colorectal cancer cells via an IGF independent pathway. The biological effects of IGF-BP4 can be regulated by Pregnancy Associated Plasma Protein A (PAPP-A), which reduces IGF-BP4/IGF binding affinity by proteolytically cleaving IGF-BP4. The modulation of IGF-BP4 activity by PAPP-A is an important component in the regulation of ovarian folliculogenesis and in the growth inhibition of responding ovarian cancer cells. Recombinant human IGF-BP4 is a 26.1 kDa protein consisting of 238 amino acid residues including the IGF-BP domain and thyroglobulin type-I domain.
Description: IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP4 is the major IGF-BP produced by osteoblasts, and is also found in the epidermis, ovarian follicles, and other tissues. IGF-BP4 inhibits the activity of IGF-I and IGF-II by binding in a manner that results in the formation of complexes with reduced ability to signal through cell surface IGF receptors. IGF-BP4 can inhibit the growth of chick pelvis cartilage and HT29 colon adenocarcinoma cells by blocking the mitogenic actions of IGFs, and has also been shown to reduce colony formation by colorectal cancer cells via an IGF independent pathway. The biological effects of IGF-BP4 can be regulated by Pregnancy Associated Plasma Protein A (PAPP-A), which reduces IGF-BP4/IGF binding affinity by proteolytically cleaving IGF-BP4. The modulation of IGF-BP4 activity by PAPP-A is an important component in the regulation of ovarian folliculogenesis and in the growth inhibition of responding ovarian cancer cells. Recombinant human IGF-BP4 is a 26.1 kDa protein consisting of 238 amino acid residues including the IGF-BP domain and thyroglobulin type-I domain.
Description: IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP4 is the major IGF-BP produced by osteoblasts, and is also found in the epidermis, ovarian follicles, and other tissues. IGF-BP4 inhibits the activity of IGF-I and IGF-II by binding in a manner that results in the formation of complexes with reduced ability to signal through cell surface IGF receptors. IGF-BP4 can inhibit the growth of chick pelvis cartilage and HT29 colon adenocarcinoma cells by blocking the mitogenic actions of IGFs, and has also been shown to reduce colony formation by colorectal cancer cells via an IGF independent pathway. The biological effects of IGF-BP4 can be regulated by Pregnancy Associated Plasma Protein A (PAPP-A), which reduces IGF-BP4/IGF binding affinity by proteolytically cleaving IGF-BP4. The modulation of IGF-BP4 activity by PAPP-A is an important component in the regulation of ovarian folliculogenesis and in the growth inhibition of responding ovarian cancer cells. Recombinant human IGF-BP4 is a 25.8 kDa protein consisting of 237 amino acid residues including the IGF-BP domain and thyroglobulin type-I domain.
*Manufactured using (BTI-Tn-5B1-4) cells under license from the Boyce Thompson Institute for Plant Research, Inc.
Description: IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP4 is the major IGF-BP produced by osteoblasts, and is also found in the epidermis, ovarian follicles, and other tissues. IGF-BP4 inhibits the activity of IGF-I and IGF-II by binding in a manner that results in the formation of complexes with reduced ability to signal through cell surface IGF receptors. IGF-BP4 can inhibit the growth of chick pelvis cartilage and HT29 colon adenocarcinoma cells by blocking the mitogenic actions of IGFs, and has also been shown to reduce colony formation by colorectal cancer cells via an IGF independent pathway. The biological effects of IGF-BP4 can be regulated by Pregnancy Associated Plasma Protein A (PAPP-A), which reduces IGF-BP4/IGF binding affinity by proteolytically cleaving IGF-BP4. The modulation of IGF-BP4 activity by PAPP-A is an important component in the regulation of ovarian folliculogenesis and in the growth inhibition of responding ovarian cancer cells. Recombinant human IGF-BP4 is a 25.8 kDa protein consisting of 237 amino acid residues including the IGF-BP domain and thyroglobulin type-I domain.
Description: IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP4 is the major IGF-BP produced by osteoblasts, and is also found in the epidermis, ovarian follicles, and other tissues. IGF-BP4 inhibits the activity of IGF-I and IGF-II by binding in a manner that results in the formation of complexes with reduced ability to signal through cell surface IGF receptors. IGF-BP4 can inhibit the growth of chick pelvis cartilage and HT29 colon adenocarcinoma cells by blocking the mitogenic actions of IGFs, and has also been shown to reduce colony formation by colorectal cancer cells via an IGF independent pathway. The biological effects of IGF-BP4 can be regulated by Pregnancy Associated Plasma Protein A (PAPP-A), which reduces IGF-BP4/IGF binding affinity by proteolytically cleaving IGF-BP4. The modulation of IGF-BP4 activity by PAPP-A is an important component in the regulation of ovarian folliculogenesis and in the growth inhibition of responding ovarian cancer cells. Recombinant human IGF-BP4 is a 25.8 kDa protein consisting of 237 amino acid residues including the IGF-BP domain and thyroglobulin type-I domain.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: Insulin-like growth factor (IGF)-I (also known as somatomedin C and somatomedin A) and IGF-II (multiplication stimulating activity or MSA) belong to the family of insulin-like growth factors that are structurally homologous to proinsulin. Mature IGF-I and IGF-II share approximately 70% sequence identity. Both IGF-I and IGF-II are expressed in many tissues and cell types and may have autocrine, paracrine and endocrine functions. Mature IGF-I and IGF-II are highly conserved between the human, bovine and porcine proteins (100% identity), and exhibit cross-species activity.
Description: Insulin-like growth factor (IGF)-I (also known as somatomedin C and somatomedin A) and IGF-II (multiplication stimulating activity or MSA) belong to the family of insulin-like growth factors that are structurally homologous to proinsulin. Mature IGF-I and IGF-II share approximately 70% sequence identity. Both IGF-I and IGF-II are expressed in many tissues and cell types and may have autocrine, paracrine and endocrine functions. Mature IGF-I and IGF-II are highly conserved between the human, bovine and porcine proteins (100% identity), and exhibit cross-species activity.
Description: Insulin-like growth factor (IGF)-I (also known as somatomedin C and somatomedin A) and IGF-II (multiplication stimulating activity or MSA) belong to the family of insulin-like growth factors that are structurally homologous to proinsulin. Mature IGF-I and IGF-II share approximately 70% sequence identity. Both IGF-I and IGF-II are expressed in many tissues and cell types and may have autocrine, paracrine and endocrine functions. Mature IGF-I and IGF-II are highly conserved between the human, bovine and porcine proteins (100% identity), and exhibit cross-species activity.
Description: Insulin-like growth factor (IGF)-I (also known as somatomedin C and somatomedin A) and IGF-II (multiplication stimulating activity or MSA) belong to the family of insulin-like growth factors that are structurally homologous to proinsulin. Mature IGF-I and IGF-II share approximately 70% sequence identity. Both IGF-I and IGF-II are expressed in many tissues and cell types and may have autocrine, paracrine and endocrine functions. Mature IGF-I and IGF-II are highly conserved between the human, bovine and porcine proteins (100% identity), and exhibit cross-species activity.
Insulin-Like Growth Factor II, Recombinant, Human (Human IGF-II, IGF-II, IGFII, IGFII, IGF2, IGF-2, IGF 2)
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to ATTO 565.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to ATTO 633.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to ATTO 655.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to ATTO 680.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to ATTO 700.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to APC/Cy7.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to Dylight 350.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to Dylight 405.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to Dylight 488.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to Dylight 594.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to Dylight 633.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to PE/ATTO 594.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to Streptavidin.
Description: Recombinant Human Cytotoxic T-lymphocyte Protein 4 is produced by our Mammalian expression system and the target gene encoding Lys36-Asp161 is expressed with a Flag tag at the C-terminus.
Zapalenie skórno-mięśniowe z dodatnim przeciwciałem anty-MDA5 z szybko postępującą śródmiąższową chorobą płuc: opis dwóch przypadków
Ar melanomas diferenciāciju saistītais proteīns 5 (MDA5) antivielu pozitīvais dermatomiozīts (DM) parāda unikālas ādas un patoloģiskās iezīmes. Mēs aprakstām divus ar miozītu saistītas ātri progresējošas intersticiālas plaušu slimības (RP-ILD) gadījumus.
Pacientes bija divas sievietes no Keralas, Indijā. Abiem pacientiem bija anti-MDA5 antivielu pozitīvs miozīts. Abiem pacientiem bija RP-ILD bez jebkādām miozīta klīniskām pazīmēm un viņi pakļāvās savai slimībai, neraugoties uz agresīvu ārstēšanu. Anti-MDA5-antivielu pozitīvam DM raksturīga amiopātiska slimība ar strauji progresējošu un letālu ILD.
Przeciwciała przeciwko dekarboksylazie glutaminianowej w surowicy a zaburzenia neurologiczne: kiedy podejrzewać ich związek?
Mērķi: Izpētīt dažādas neiroloģiskas izpausmes ar aizdomām par saistību ar seruma glutamāta dekarboksilāzes antivielām (GAD-Abs), lai labāk raksturotu anti-GAD neiroloģiskos sindromus.
Metodes: Novērošanas retrospektīvais pētījums, kurā tika iekļauti visi pacienti, kuriem La Pazas Universitātes slimnīcas Neiroloģijas nodaļa laika posmā no 2015. līdz 2019. gadam pieprasīja GAD65-Abs titru serumā. GAD-Abs mērīja ar ELISA. Tika pētīti demogrāfiskie dati, neiroloģiskie simptomi, blakusslimības ar cukura diabētu (DM) vai citu autoimūno slimību un GAD-Abs titri. Stingras personas sindroms, ataksija, encefalīts un epilepsija tika uzskatīti par tipiskiem anti-GAD neiroloģiskiem sindromiem un tika salīdzināti ar citām netipiskām izpausmēm.
Rezultāti: Kopumā tika iekļauti 173 pacienti (51,7% vīriešu, vidējais vecums 51,62). Pēdējo 5 gadu laikā pakāpeniski palielinājās seruma GAD-Abs pieprasījumu skaits, īpaši pacientiem ar netipiskām neiroloģiskām izpausmēm. GAD-Abs tika konstatēti 22 pacientu serumā (12,7%); no tiem 15 (68,18%) cieta tipisku anti-GAD sindromu.
DM vai citas orgānspecifiskas autoimūnas slimības klātbūtne paredzēja GAD-AB seropozitivitāti (p <0,001). 6,6% no pieprasītajiem pacientiem ar netipisku sindromu bija GAD-Abs, guess seruma līmenis bija ievērojami zemāks nekā konstatēts pacientiem ar tipisku sindromu (706,67 vs 1430,23 UI / ml; Mann-Whitney U, p = 0,034), un beidzot diagnosticēta cita neiroloģiska slimība.
Secinājums: serumā GAD-Abs reti tika konstatēti pacienti ar klīniskiem fenotipiem, izņemot tos, kas klasiski aprakstīti kā anti-GAD traucējumi, un ar ļoti zemu titru. Tipiskos anti-GAD sindromos ir augsta saslimstība ar DM un citām autoimūnām slimībām, un parasti ir augsts GAD-Abs līmenis serumā.
Podwójne dodatnie wyniki przeciwciał przeciwko β 2 -glikoproteinie I domenie I i przeciw fosfatydyloserynie / protrombinie wzmacniają zarówno zakrzepicę, jak i dodatni wynik przeciwciał anty-ADAMTS
Lai gan ar iegūto trombotisko trombocitopēnisko purpuru (TTP) rodas daži antifosfolipīdu sindromi (APS), saistība starp antifosfolipīdu antivielām (aPL) un anti-ADAMTS13 (anti-a dezintegrīnu un metalloproteāzi ar 1. tipa trombospondīna motīvu, 13. loceklis) paliek nenoteikta.
Mēs pētījām saikni starp augsta riska trombotisko aPL un anti-ADAMTS13 antivielām. Tika iekļauti divi simti trīsdesmit septiņi pacienti ar pozitīvu vilkēdes antikoagulantu un / vai antikardiolipīna antivielu. Tika izmērīti anti-β2GPI (anti-β2-glikoproteīns I), anti-β2GPIdI (anti-β2-glikoproteīna I domēns I), anti-PS / PT (antifosfatidilserīns un protrombīns), ADAMTS13 aktivitāte un anti-ADAMTS13 antiviela.
Divkārša anti-β2GPI un anti-PS / PT pozitivitāte palielināja trombozes risku vairāk nekā trīs reizes un parādīja paaugstinātu anti-ADAMTS13 antivielu pozitivitāti, salīdzinot ar dubultnegatīvo grupu.
Dubultā pozitīvā anti-β2GPIdI un anti-PS / PT parādīja abus efektus vēl vairāk. Lineārajā regresijas analīzē anti-β2GPI un anti-PS / PT dubultā pozitivitāte neatkarīgi ietekmēja antivielu līmeni anti-ADAMTS13 (β = 1,982, P = 0,042).
Mūsu rezultāti atklāja, ka anti-β2GPI vai anti-β2GPIdI un anti-PS / PT dubultā pozitivitāte palielināja ne tikai trombotisko risku, guess arī anti-ADAMTS13 antivielu pozitivitāti, īpaši norādot, ka anti-β2GPIdI parādīja augstāku sinerģisko efektu ar anti-PS / PT.
Mēs iesakām iespējamu anti-ADAMTS13 antivielu saistību ar augstu APS trombotisko risku.
Anti-β2GPI (anti-β2-glikoproteīns I) un anti-PS / PT (anti-fosfatidilserīns un protrombīns) antivielu dubultā pozitivitāte palielināja ne tikai trombotisko risku, guess arī anti-ADAMTS13 (anti-dezintegrīna un metaloproteāzes ar trombospondīna tipa) pozitivitāti 1 motīvs, loceklis 13) antivielas.
Turklāt anti-β2GPIdI (anti-β2-glikoproteīna I domēns I) dubultā pozitivitāte kombinācijā ar anti-PS / PT vēl vairāk paaugstināja gan trombozi, gan anti-ADAMTS13 antivielu pozitivitāti. Tika konstatēts, ka dubultā pozitivitāte β2GPI un anti-PS / PT kā neatkarīgi nozīmīgs faktors anti-ADAMTS13 antivielu līmeņa paaugstināšanai. Mēs iesakām saistību starp anti-ADAMTS13 antivielām un antifosfolipīdu sindroma patofizioloģiju, kas būtu tālāk jāizvērtē.
