Transcortin: Difference between revisions

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Latest revision as of 06:20, 10 January 2019

Transcortin, also known as corticosteroid-binding globulin (CBG) or serpin A6, is a protein that in humans is encoded by the SERPINA6 gene. It is an alpha-globulin.^[1]^[2]^[3]

Function

This gene encodes an alpha-globulin protein with corticosteroid-binding properties. This is the major transport protein for glucocorticoids and progestins in the blood of most vertebrates. The gene localizes to a chromosomal region containing several closely related serine protease inhibitors (serpins) which have evolved by duplication events.^[3]

Binding

Transcortin binds several steroid hormones at high rates:

Cortisol - Approximately 75% of the cortisol in circulation is bound to transcortin. (The rest is bound to serum albumin.) Cortisol is thought to be biologically active only when it is not bound to transcortin.^{[citation needed]}
Cortisone^[4]
Deoxycorticosterone (DOC)^[4]
Corticosterone - About 78% of serum corticosterone is bound to transcortin.
Aldosterone - Approximately 17% of serum aldosterone is bound to transcortin, while another 47% is bound to serum albumin. The remaining 36% is free.^[5]
Progesterone - Approximately 18% of serum progesterone is bound to transcortin, while another 80% of it is bound to serum albumin. The remaining 2% is free.^[6]
17α-Hydroxyprogesterone^[4]

In addition, approximately 4% of serum testosterone is bound to transcortin.^[7] A similarly small fraction of serum estradiol is bound to transcortin as well.^{[citation needed]}

Synthesis

Transcortin is produced by the liver and is increased by estrogens.^[8]

Clinical significance

Mutations in this gene are rare. Only four mutations have been described, often in association with fatigue and chronic pain.^[9] This mechanism for these symptoms is not known. This condition must be distinguished from secondary hypocortisolism. Exogenous hydrocortisone does not appear to improve the fatigue.

Hepatic synthesis of corticosteroid-binding globulin more than doubles in pregnancy; that is, unbound plasma cortisol in term pregnancy is approximately 2.5 times that of nonpregnant women.^[10]

References

↑ Hammond GL, Smith CL, Goping IS, Underhill DA, Harley MJ, Reventos J, Musto NA, Gunsalus GL, Bardin CW (August 1987). "Primary structure of human corticosteroid binding globulin, deduced from hepatic and pulmonary cDNAs, exhibits homology with serine protease inhibitors". Proc Natl Acad Sci U S A. 84 (15): 5153–7. doi:10.1073/pnas.84.15.5153. PMC 298812. PMID 3299377.
↑ Byth BC, Billingsley GD, Cox DW (July 1994). "Physical and genetic mapping of the serpin gene cluster at 14q32.1: allelic association and a unique haplotype associated with alpha 1-antitrypsin deficiency". Am J Hum Genet. 55 (1): 126–33. PMC 1918218. PMID 7912884.
↑ ^3.0 ^3.1 "Entrez Gene: SERPINA6 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 6".
↑ ^4.0 ^4.1 ^4.2 E. Edward Bittar; Neville Bittar (1997). Molecular and Cellular Endocrinology. Elsevier. p. 238. ISBN 978-1-55938-815-3. Retrieved 23 August 2012.
↑ Principles and Practice of Endocrinology and Metabolism. Lippincott Williams & Wilkins. 24 April 2001. p. 712. ISBN 978-0-7817-1750-2. Retrieved 23 August 2012.
↑ Negi (2009). Introduction To Endocrinology. PHI Learning Pvt. Ltd. p. 268. ISBN 978-81-203-3850-0. Retrieved 23 August 2012.
↑ Dunn JF, Nisula BC, Rodbard D (July 1981). "Transport of steroid hormones: binding of 21 endogenous steroids to both testosterone-binding globulin and corticosteroid-binding globulin in human plasma". The Journal of Clinical Endocrinology and Metabolism. 53 (1): 58–68. doi:10.1210/jcem-53-1-58. PMID 7195404.
↑ Musa BU, Seal US, Doe RP (September 1965). "Elevation of certain plasma proteins in man following estrogen administration: a dose-response relationship". J. Clin. Endocrinol. Metab. 25 (9): 1163–6. doi:10.1210/jcem-25-9-1163. PMID 4284083.
↑ Torpy DJ, Lundgren BA, Ho JT, Lewis JG, Scott HS, Mericq V (January 2012). "CBG Santiago: a novel CBG mutation". J. Clin. Endocrinol. Metab. 97 (1): E151–5. doi:10.1210/jc.2011-2022. PMID 22013108.
↑ Rosen MI, Shnider SM, Levinson G, Hughes (2002). Shnider and Levinson's anesthesia for obstetrics. Hagerstwon, MD: Lippincott Williams & Wilkins. p. 13. ISBN 0-683-30665-0.

External links

Transcortin at the US National Library of Medicine Medical Subject Headings (MeSH)
The MEROPS online database for peptidases and their inhibitors: I04.954
SERPINA6+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)

[pmid3299377-1] Hammond GL, Smith CL, Goping IS, Underhill DA, Harley MJ, Reventos J, Musto NA, Gunsalus GL, Bardin CW (August 1987). "Primary structure of human corticosteroid binding globulin, deduced from hepatic and pulmonary cDNAs, exhibits homology with serine protease inhibitors". Proc Natl Acad Sci U S A. 84 (15): 5153–7. doi:10.1073/pnas.84.15.5153. PMC 298812. PMID 3299377.

[pmid7912884-2] Byth BC, Billingsley GD, Cox DW (July 1994). "Physical and genetic mapping of the serpin gene cluster at 14q32.1: allelic association and a unique haplotype associated with alpha 1-antitrypsin deficiency". Am J Hum Genet. 55 (1): 126–33. PMC 1918218. PMID 7912884.

[entrez-3] 3.0 ^3.1 "Entrez Gene: SERPINA6 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 6".

[BittarBittar1997-4] 4.0 ^4.1 ^4.2 E. Edward Bittar; Neville Bittar (1997). Molecular and Cellular Endocrinology. Elsevier. p. 238. ISBN 978-1-55938-815-3. Retrieved 23 August 2012.

[Principles_and_Practice_of_Endocrinology_and_Metabolism-5] Principles and Practice of Endocrinology and Metabolism. Lippincott Williams & Wilkins. 24 April 2001. p. 712. ISBN 978-0-7817-1750-2. Retrieved 23 August 2012.

[Negi2009-6] Negi (2009). Introduction To Endocrinology. PHI Learning Pvt. Ltd. p. 268. ISBN 978-81-203-3850-0. Retrieved 23 August 2012.

[pmid7195404-7] Dunn JF, Nisula BC, Rodbard D (July 1981). "Transport of steroid hormones: binding of 21 endogenous steroids to both testosterone-binding globulin and corticosteroid-binding globulin in human plasma". The Journal of Clinical Endocrinology and Metabolism. 53 (1): 58–68. doi:10.1210/jcem-53-1-58. PMID 7195404.

[pmid4284083-8] Musa BU, Seal US, Doe RP (September 1965). "Elevation of certain plasma proteins in man following estrogen administration: a dose-response relationship". J. Clin. Endocrinol. Metab. 25 (9): 1163–6. doi:10.1210/jcem-25-9-1163. PMID 4284083.

[pmid22013108-9] Torpy DJ, Lundgren BA, Ho JT, Lewis JG, Scott HS, Mericq V (January 2012). "CBG Santiago: a novel CBG mutation". J. Clin. Endocrinol. Metab. 97 (1): E151–5. doi:10.1210/jc.2011-2022. PMID 22013108.

[isbn0-683-30665-0-10] Rosen MI, Shnider SM, Levinson G, Hughes (2002). Shnider and Levinson's anesthesia for obstetrics. Hagerstwon, MD: Lippincott Williams & Wilkins. p. 13. ISBN 0-683-30665-0.

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@@ Line 1: / Line 1: @@
-{{Protein
+{{Infobox gene}}
-   |Name=Serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 6, also Corticosteroid-Binding Globulin or Transcortin
+'''Transcortin''', also known as '''corticosteroid-binding globulin''' (CBG) or '''serpin A6''', is a [[protein]] that in humans is encoded by the SERPINA6 [[gene]]. It is an [[alpha-globulin]].<ref name="pmid3299377">{{cite journal |vauthors=Hammond GL, Smith CL, Goping IS, Underhill DA, Harley MJ, Reventos J, Musto NA, Gunsalus GL, Bardin CW | title = Primary structure of human corticosteroid binding globulin, deduced from hepatic and pulmonary cDNAs, exhibits homology with serine protease inhibitors | journal = Proc Natl Acad Sci U S A | volume = 84 | issue = 15 | pages = 5153–7 |date=August 1987 | pmid = 3299377 | pmc = 298812 | doi =10.1073/pnas.84.15.5153  }}</ref><ref name="pmid7912884">{{cite journal |vauthors=Byth BC, Billingsley GD, Cox DW | title = Physical and genetic mapping of the serpin gene cluster at 14q32.1: allelic association and a unique haplotype associated with alpha 1-antitrypsin deficiency | journal = Am J Hum Genet | volume = 55 | issue = 1 | pages = 126–33 |date=July 1994 | pmid = 7912884 | pmc = 1918218 | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: SERPINA6 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 6| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=866| accessdate = }}</ref>
-   |image=
-   |caption=
-   |Symbol=SERPINA6
-   |AltSymbols= CBG
-   |HGNCid=1540
-   |Chromosome=14
-   |Arm=q
-   |Band=32.1
-   |LocusSupplementaryData=
-   |ECnumber=
-   |OMIM=122500
-   |EntrezGene=866
-   |RefSeq=NM_001750
-   |UniProt=P08185
-   |PDB=
-}}
-{{SI}}
-{{CMG}}
-{{EH}}
+== Function ==
-==Overview==
+This gene encodes an [[alpha-globulin]] protein with [[corticosteroid]]-binding properties. This is the major transport protein for [[glucocorticoid]]s and [[progestin]]s in the blood of most vertebrates. The gene localizes to a chromosomal region containing several closely related serine protease inhibitors ([[serpin]]s) which have evolved by duplication events.<ref name="entrez"/>
-'''Transcortin''', also '''corticosteroid-binding globulin''' or '''CBG''', is officially called '''serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 6'''.
-It is an [[alpha-globulin]].
+==Binding==
+Transcortin binds several steroid hormones at high rates:
-==Binding==
+* [[Cortisol]] - Approximately 75% of the cortisol in circulation is bound to transcortin. (The rest is bound to [[serum albumin]].) Cortisol is thought to be biologically active only when it is not bound to transcortin.{{citation needed|date=March 2016}}
-Transcortin binds several proteins:
+* [[Cortisone]]<ref name="BittarBittar1997">{{cite book | author1 = E. Edward Bittar | author2 = Neville Bittar | title = Molecular and Cellular Endocrinology | url = https://books.google.com/books?id=sSHhmGqyXhcC&pg=PA238 | accessdate = 23 August 2012 | year = 1997 | publisher = Elsevier | isbn = 978-1-55938-815-3 | page = 238}}</ref>
+* [[11-Deoxycorticosterone|Deoxycorticosterone]] (DOC)<ref name="BittarBittar1997" />
+* [[Corticosterone]] - About 78% of serum corticosterone is bound to transcortin.
+* [[Aldosterone]] - Approximately 17% of serum aldosterone is bound to transcortin, while another 47% is bound to serum albumin. The remaining 36% is free.<ref name="Principles and Practice of Endocrinology and Metabolism">{{cite book | title = Principles and Practice of Endocrinology and Metabolism | url = https://books.google.com/books?id=FVfzRvaucq8C&pg=PA712 | accessdate = 23 August 2012 | date = 24 April 2001 | publisher = Lippincott Williams & Wilkins | isbn = 978-0-7817-1750-2 | page = 712}}</ref>
+* [[Progesterone]] - Approximately 18% of serum progesterone is bound to transcortin, while another 80% of it is bound to serum albumin. The remaining 2% is free.<ref name="Negi2009">{{cite book | author = Negi | title = Introduction To Endocrinology | url = https://books.google.com/books?id=7Ev2mV4c_vUC&pg=PA268 | accessdate = 23 August 2012 | year = 2009 | publisher = PHI Learning Pvt. Ltd. | isbn = 978-81-203-3850-0 | page = 268}}</ref>
+* [[17α-Hydroxyprogesterone]]<ref name="BittarBittar1997" />
-* [[Cortisol]]. Approximately 75% of the cortisol in circulation is bound to this plasma protein. (The rest is bound to [[serum albumin]].) The cortisol is thought to be biologically active only when it is not bound to transcortin.
+In addition, approximately 4% of serum [[testosterone]] is bound to transcortin.<ref name="pmid7195404">{{cite journal |vauthors=Dunn JF, Nisula BC, Rodbard D | title = Transport of steroid hormones: binding of 21 endogenous steroids to both testosterone-binding globulin and corticosteroid-binding globulin in human plasma | journal = The Journal of Clinical Endocrinology and Metabolism | volume = 53 | issue = 1 | pages = 58–68 |date=July 1981 | pmid = 7195404 | doi = 10.1210/jcem-53-1-58| url = http://jcem.endojournals.org/cgi/pmidlookup?view=long&pmid=7195404}}</ref> A similarly small fraction of serum [[estradiol]] is bound to transcortin as well.{{Citation needed|date=August 2012}}
-* [[Aldosterone]]. 60% of the aldosterone in blood is bound to this plasma protein.
+== Synthesis ==
+Transcortin is produced by the [[liver]] and is increased by [[estrogen]]s.<ref name="pmid4284083">{{cite journal |vauthors=Musa BU, Seal US, Doe RP | title = Elevation of certain plasma proteins in man following estrogen administration: a dose-response relationship | journal = J. Clin. Endocrinol. Metab. | volume = 25 | issue = 9 | pages = 1163–6 |date=September 1965 | pmid = 4284083 | doi = 10.1210/jcem-25-9-1163 }}</ref>
-* [[Progesterone]]
+== Clinical significance ==
+Mutations in this gene are rare. Only four mutations have been described, often in association with fatigue and chronic pain.<ref name="pmid22013108">{{cite journal |vauthors=Torpy DJ, Lundgren BA, Ho JT, Lewis JG, Scott HS, Mericq V | title = CBG Santiago: a novel CBG mutation | journal = J. Clin. Endocrinol. Metab. | volume = 97 | issue = 1 | pages = E151–5 |date=January 2012 | pmid = 22013108 | doi = 10.1210/jc.2011-2022 }}</ref> This mechanism for these symptoms is not known. This condition must be distinguished from secondary hypocortisolism.  Exogenous hydrocortisone does not appear to improve the fatigue.
-==Production==
+Hepatic synthesis of corticosteroid-binding globulin more than doubles in pregnancy; that is, unbound plasma cortisol in term pregnancy is approximately 2.5 times that of nonpregnant women.<ref name="isbn0-683-30665-0">{{cite book | author = Rosen MI, Shnider SM, Levinson G, Hughes  | title = Shnider and Levinson's anesthesia for obstetrics | publisher = Lippincott Williams & Wilkins | location = Hagerstwon, MD | year = 2002 | page = 13 | isbn = 0-683-30665-0 }}</ref>
-Transcortin is produced by the [[liver]] and is regulated by [[estrogen]]s.  Therefore, plasma transcortin levels increase during [[pregnancy]], and are decreased in [[cirrhosis]].
 ==See also==
-* [[Sex hormone binding globulin]]
 * [[Serpin]]
+* [[Circaseptan]], 7-day biological cycle
+== References ==
+{{reflist}}
-==External links==
+==Further reading==
+{{refbegin | 2}}
+*{{cite journal  |vauthors=Rosner W, Beers PC, Awan T, Khan MS |title=Identification of corticosteroid-binding globulin in human milk: measurement with a filter disk assay. |journal=J. Clin. Endocrinol. Metab. |volume=42 |issue= 6 |pages= 1064–73 |year= 1976 |pmid= 932172 |doi=10.1210/jcem-42-6-1064  }}
+*{{cite journal  |vauthors=Smith CL, Power SG, Hammond GL |title=A Leu----His substitution at residue 93 in human corticosteroid binding globulin results in reduced affinity for cortisol. |journal=J. Steroid Biochem. Mol. Biol. |volume=42 |issue= 7 |pages= 671–6 |year= 1992 |pmid= 1504007 |doi=10.1016/0960-0760(92)90107-T  }}
+*{{cite journal  | author=Brotherton J |title=Cortisol and transcortin in human seminal plasma and amniotic fluid as estimated by modern specific assays. |journal=Andrologia |volume=22 |issue= 3 |pages= 197–204 |year= 1990 |pmid= 2240617 |doi=10.1111/j.1439-0272.1990.tb01966.x  }}
+*{{cite journal  |vauthors=Seralini GE, Bérubé D, Gagné R, Hammond GL |title=The human corticosteroid binding globulin gene is located on chromosome 14q31-q32.1 near two other serine protease inhibitor genes. |journal=Hum. Genet. |volume=86 |issue= 1 |pages= 73–5 |year= 1991 |pmid= 2253941 |doi=  10.1007/bf00205177}}
+*{{cite journal  |vauthors=Underhill DA, Hammond GL |title=Organization of the human corticosteroid binding globulin gene and analysis of its 5'-flanking region. |journal=Mol. Endocrinol. |volume=3 |issue= 9 |pages= 1448–54 |year= 1990 |pmid= 2608068 |doi=10.1210/mend-3-9-1448  }}
+*{{cite journal   |vauthors=Loric S, Egloff M, Domingo M, etal |title=Immunochemical characterization of corticosteroid-binding globulin in human bronchoalveolar fluid. |journal=Clin. Chim. Acta |volume=186 |issue= 1 |pages= 19–23 |year= 1990 |pmid= 2612005 |doi=10.1016/0009-8981(89)90198-8  }}
+*{{cite journal   |vauthors=Heubner A, Belovsky O, Müller W, etal |title=Application of liquid-liquid partition chromatography in the simultaneous purification of sex-hormone-binding globulin and corticosteroid-binding globulin. |journal=J. Chromatogr. |volume=397 |issue=  |pages= 419–34 |year= 1987 |pmid= 2821037 |doi=10.1016/S0021-9673(01)85027-5  }}
+*{{cite journal  |vauthors=Kato EA, Hsu BR, Kuhn RW |title=Comparative structural analyses of corticosteroid binding globulin. |journal=J. Steroid Biochem. |volume=29 |issue= 2 |pages= 213–20 |year= 1988 |pmid= 3347061 |doi=10.1016/0022-4731(88)90268-3  }}
+*{{cite journal   |vauthors=Bardin CW, Gunsalus GL, Musto NA, etal |title=Corticosteroid binding globulin, testosterone-estradiol binding globulin, and androgen binding protein belong to protein families distinct from steroid receptors. |journal=J. Steroid Biochem. |volume=30 |issue= 1-6 |pages= 131–9 |year= 1988 |pmid= 3386241 |doi=10.1016/0022-4731(88)90085-4  }}
+*{{cite journal  |vauthors=Hammond GL, Langley MS |title=Identification and measurement of sex hormone binding globulin (SHBG) and corticosteroid binding globulin (CBG) in human saliva. |journal=Acta Endocrinol. |volume=112 |issue= 4 |pages= 603–8 |year= 1986 |pmid= 3751467 |doi=  10.1530/acta.0.1120603}}
+*{{cite journal   |vauthors=Agrimonti F, Frairia R, Fornaro D, etal |title=Circadian and [[circaseptan]] rhythmicities in corticosteroid-binding globulin (CBG) binding activity of human milk. |journal=Chronobiologia |volume=9 |issue= 3 |pages= 281–90 |year= 1983 |pmid= 7172869 |doi=  }}
+*{{cite journal   |vauthors=Misao R, Hori M, Ichigo S, etal |title=Levels of sex hormone-binding globulin (SHBG) and corticosteroid-binding globulin (CBG) messenger ribonucleic acid (mRNAs) in ovarian endometriosis. |journal=Reprod. Nutr. Dev. |volume=35 |issue= 2 |pages= 155–65 |year= 1995 |pmid= 7734053 |doi=10.1051/rnd:19950204  }}
+*{{cite journal   |vauthors=Misao R, Hori M, Ichigo S, etal |title=Corticosteroid-binding globulin mRNA levels in human uterine endometrium. |journal=Steroids |volume=59 |issue= 10 |pages= 603–7 |year= 1995 |pmid= 7878688 |doi=10.1016/0039-128X(94)90055-8  }}
+*{{cite journal  |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
+*{{cite journal  |vauthors=Avvakumov GV, Hammond GL |title=Glycosylation of human corticosteroid-binding globulin. Differential processing and significance of carbohydrate chains at individual sites. |journal=Biochemistry |volume=33 |issue= 19 |pages= 5759–65 |year= 1994 |pmid= 8180202 |doi=10.1021/bi00185a012  }}
+*{{cite journal  |vauthors=Van Baelen H, Power SG, Hammond GL |title=Decreased cortisol-binding affinity of transcortin Leuven is associated with an amino acid substitution at residue-93. |journal=Steroids |volume=58 |issue= 6 |pages= 275–7 |year= 1993 |pmid= 8212073 |doi=10.1016/0039-128X(93)90072-U  }}
+*{{cite journal   |vauthors=Misao R, Nakanishi Y, Fujimoto J, etal |title=Expression of corticosteroid-binding globulin mRNA in human uterine endometrial cancers. |journal=Steroids |volume=60 |issue= 10 |pages= 720–4 |year= 1996 |pmid= 8539782 |doi=10.1016/0039-128X(95)00106-Z  }}
+*{{cite journal   |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  }}
+{{refend}}
+== External links ==
 * {{MeshName|Transcortin}}
+* The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=I04.954 I04.954]
+* {{MeshName|SERPINA6+protein,+human}}
 {{Carrier proteins}}
@@ Line 49: / Line 64: @@
 {{Serpins}}
 {{Glycoproteins}}
-{{SIB}}
+{{Glucocorticoidics}}
+{{Mineralocorticoidics}}
-[[category:Glycoproteins]]
+{{Progestogenics}}
+{{Use dmy dates|date=April 2017}}
-[[de:Transcortin]]
-[[fr:Transcortine]]
-[[Category:Proteins]]
-{{WikiDoc Help Menu}}
+[[Category:Glycoproteins]]
-{{WikiDoc Sources}}

v t e Proteins: carrier proteins
Fatty acid	FABP1 FABP2 FABP3 FABP4 FABP5 FABP6 FABP7
Hormone	peptide hormone: Follistatin Growth hormone binding protein Insulin-like growth factor binding protein IGFBP1 IGFBP2 IGFBP3 IGFBP4 IGFBP5 IGFBP6 IGFBP7 Neurophysins Neurophysin I II steroid hormone: Sex hormone binding globulin/Androgen binding protein Transcortin Thyroxine-binding globulin Transthyretin
Metal/element	calcium Calcium-binding protein Calmodulin-binding proteins copper Ceruloplasmin iron Iron-binding proteins Transferrin receptor
Vitamin	Retinol binding protein 1 2 3 4 Transcobalamin
Pigment	Plant Light-Harvesting Complex Orange Carotenoid Protein Phycobiliprotein Photosynthetic Reaction Centers Phytochrome Rhodopsin
Other	Acyl carrier protein Adaptor protein Cholesterylester transfer protein F-box protein GTP-binding protein Latent TGF-beta binding protein Major urinary proteins Membrane transport protein Odorant binding protein

v t e Serpins
inhibitory	Alpha 1-antichymotrypsin Alpha 1-antitrypsin Alpha 2-antiplasmin Antithrombin C1-inhibitor Heparin cofactor II Protein C inhibitor Plasminogen activator inhibitor-1 Plasminogen activator inhibitor-2 Protein Z-related protease inhibitor SERPINA1 SERPINA2 SERPINA3 SERPINA4 SERPINA5 SERPINA9 SERPINA14 SERPINB1 SERPINB2 SERPINB3 SERPINB4 SERPINB5 SERPINB6 SERPINB7 SERPINB8 SERPINB9 SERPINB13 SERPINC1 SERPIND1 SERPINE1 SERPINE2 SERPINE2 SERPINF1 SERPING1 SERPINH1 SERPINI1 SERPINI2
Cross class inhibitory	MENT SCCA-1 CrmA
noninhibitory	Heat shock protein 47 Maspin Ovalbumin SERPINF1 Transcortin Thyroxine-binding globulin Angiotensinogen SERPINF1
see also disorders of globin and globulin proteins

Transcortin: Difference between revisions

Latest revision as of 06:20, 10 January 2019

Contents

Function

Binding

Synthesis

Clinical significance

See also

References

Further reading

External links

Navigation menu