Human growth hormone: Difference between revisions
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HGH is phosphorylated on Ser residues 132 and 176 (Giorgianni, Beranova-Giorgianni, and Desiderio, 2004)<ref>PMID:14997482</ref>. Other research has indicated possible phosphorylation of Tyr residues 35 and 42. However, these phosphorylations were only investigated in carcinoma cells with constitutively active epidermal growth factor-stimulated tyrosine kinase (Baldwin et al., 1983)<ref>PMID:6600511</ref>. The overall influence of these post-translational modifications on hGH activity has yet to be determined. | HGH is phosphorylated on Ser residues 132 and 176 (Giorgianni, Beranova-Giorgianni, and Desiderio, 2004)<ref>PMID:14997482</ref>. Other research has indicated possible phosphorylation of Tyr residues 35 and 42. However, these phosphorylations were only investigated in carcinoma cells with constitutively active epidermal growth factor-stimulated tyrosine kinase (Baldwin et al., 1983)<ref>PMID:6600511</ref>. The overall influence of these post-translational modifications on hGH activity has yet to be determined. | ||
Glycosylation | '''Glycosylation'''<br/> | ||
Glycosylation helps distinguish between different variants and isoforms as it works as an ID cards for proteins. These carbohydrates are specific to each forms and are recognized by the associated hgH receptors. Though still being a relatively unknown mechanism in hgH, tudies have shown that one isoform in particular, a 22kDa variant was identified and discovered mostly due to the specific carbohydrates linked to the polypeptide chain. | Glycosylation helps distinguish between different variants and isoforms as it works as an ID cards for proteins. These carbohydrates are specific to each forms and are recognized by the associated hgH receptors. Though still being a relatively unknown mechanism in hgH, tudies have shown that one isoform in particular, a 22kDa variant was identified and discovered mostly due to the specific carbohydrates linked to the polypeptide chain. | ||