Degrades extracellular matrix. Proposed to play a role in breast cancer invasion and metastasis. Exhibits trypsin-like activity as defined by cleavage of synthetic substrates with Arg or Lys as the P1 site.Defects in ST14 are a cause of ichthyosis autosomal recessive with hypotrichosis (ARIH). ARIH is a skin disorder characterized by congenital ichthyosis associated with the presence of less than the normal amount of hair.
The ST6GAL1 gene encodes β-Galactosamide α-2;6-Sialyltransferase 1. It is a type II membrane protein and is localized to the trans-Golgi network. It catalyzes 2;6-sialylation of Galβ1;4-GlcNAc structures on N-glycans. ST6GAL1 is highly expressed in the liver and other tissues. ST6GAL1 deficiency causes abnormalities in B-cell immunoreactivity. The expression and activity of ST6GAL1 are associated with tumor metastasis in breast and colon cancers. The majority of ST6GAL1 in the liver is cleaved and secreted into the serum and may be used as a biomarker for hepatitis diseases.
Alpha-N-Acetylgalactosaminide α-2,6-Sialyltransferase 2 (ST6GALNAC2) belongs to the glycosyltransferase 29 family that adds sialic acids to the non-reducing ends of glycoconjugates. At the cell surface, these modifications play roles in cell-cell and cell-substrate interactions, bacterial adhesion and protein targeting. ST6GALNAC2 is localized to the Golgi apparatus membrane. ST6GALNAC2 is highly expressed in lactating mammary glands and the adult testis; it is expressed at lower levels in the kidney. ST6GALNAC2 can catalyze 2,6-sialylation of the Tn antigen.
α-N-Acetylneuraminide α-2,8-Sialyltransferase (ST8SIA1) belongs to the glycosyltransferase 29 family. ST8SIA1 is a sialytransferase that catalyzes the transfer of sialic acid from CMP-sialic acid to GM3 to produce GD3 and GT3. ST8SIA1 is highly expressed in melanoma cell lines, adult and fetal brain, low expressed in adult and fetal lung. ST8SIA1 may act as a type II transmembrane protein with a short N-termianl cytoplasmic domain and a single-pass transmembrane domain folowed by an enzymatic domain in the lument of the Golgi apparatus.
Stanniocalcin 1 (STC-1) is a homodimeric glycoprotein hormone that is involved in calcium and phosphate homeostasis. It was originally identified in bony fishes, where elevation of calcium in serum causes the release of STC from the endocrine glands called the corpuscles of Stannius. STC-1 inhibits the breakdown of PAPP-A, protects cancer cells from apoptosis, reduces tumor size of liver cancers, promotes osteoblast differentiation and inhibits longitudinal bone growth directly at the growth plate. It is also a biomarker of brain and lung cancer progression. STC1 signals through inhibitory G-protein modulates CGRP receptor spatial localization during osteoblastogenesis and may function as a regulatory factor interacting with calcitonin peptide members during bone formation.
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