Effects of the storage conditions on the stability of natural and synthetic cannabis in biological matrices for forensic toxicology analysis: An update from the literature
Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I (I and IB) and two type II (II and IIB) receptors. These receptors are all transmembrane proteins, composed of a ligand-binding extracellular domain with cysteine-rich region, a transmembrane domain, and a cytoplasmic domain with predicted serine/threonine specificity. Type I receptors are essential for signaling; and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a stable complex after ligand binding, resulting in phosphorylation of type I receptors by type II receptors. Type II receptors are considered to be constitutively active kinases. This gene encodes activin A type IIB receptor, which displays a 3- to 4-fold higher affinity for the ligand than activin A type II receptor.[7]
^De Winter JP, De Vries CJ, Van Achterberg TA, Ameerun RF, Feijen A, Sugino H, De Waele P, Huylebroeck D, Verschueren K, Van Den Eijden-Van Raaij AJ (May 1996). "Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. receptors". Exp. Cell Res. 224 (2): 323–34. doi:10.1006/excr.1996.0142. PMID8612709.
De Winter JP, De Vries CJ, Van Achterberg TA, Ameerun RF, Feijen A, Sugino H, De Waele P, Huylebroeck D, Verschueren K, Van Den Eijden-Van Raaij AJ (1996). "Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. receptors". Exp. Cell Res. 224 (2): 323–34. doi:10.1006/excr.1996.0142. PMID8612709.
McPherron AC, Lawler AM, Lee SJ (1999). "Regulation of anterior/posterior patterning of the axial skeleton by growth/differentiation factor 11". Nat. Genet. 22 (3): 260–4. doi:10.1038/10320. PMID10391213. S2CID1172738.
Bondestam J, Horelli-Kuitunen N, Hildén K, Ritvos O, Aaltonen J (1999). "Assignment of ACVR2 and ACVR2B the human activin receptor type II and IIB genes to chromosome bands 2q22.2-->q23.3 and 3p22 and the human follistatin gene (FST) to chromosome 5q11.2 by FISH". Cytogenet. Cell Genet. 87 (3–4): 219–20. doi:10.1159/000015429. PMID10702675. S2CID36135054.
Choi KC, Kang SK, Nathwani PS, Cheng KW, Auersperg N, Leung PC (2001). "Differential expression of activin/inhibin subunit and activin receptor mRNAs in normal and neoplastic ovarian surface epithelium (OSE)". Mol. Cell. Endocrinol. 174 (1–2): 99–110. doi:10.1016/S0303-7207(00)00447-0. PMID11306176. S2CID10648768.
Schneider-Kolsky ME, Manuelpillai U, Waldron K, Dole A, Wallace EM (2002). "The distribution of activin and activin receptors in gestational tissues across human pregnancy and during labour". Placenta. 23 (4): 294–302. doi:10.1053/plac.2002.0787. PMID11969340.
PDB gallery
1nys: Crystal Structure of Activin A Bound to the ECD of ActRIIB P41
1nyu: Crystal Structure of Activin A Bound to the ECD of ActRIIB
1s4y: Crystal structure of the activin/actrIIb extracellular domain
2h62: Crystal structure of a ternary ligand-receptor complex of BMP-2
2h64: Crystal structure of a ternary ligand-receptor complex of BMP-2