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Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes
It is demonstrated for the first time the importance of hydroxylysine-linked glycosylation for collagens and the reduction of the GGT activity of LH3 disrupts the localization of type IV collagen, and thus the formation of basement membranes during mouse embryogenesis leading to lethality at embryonic day 9.5.
Expanding the lysyl hydroxylase toolbox: New insights into the localization and activities of lysyl hydroxylase 3 (LH3)
It is shown that growth cone migration depends critically on the LH3 glycosyltransferase domain, but, unlike the other isoforms, LH3 is also found in the extracellular space in some tissues, suggesting that it may have a role in matrix remodeling.
Secretion and Assembly of Type IV and VI Collagens Depend on Glycosylation of Hydroxylysines*
Analysis of LH3 knock-out embryos and cells indicated that loss of glycosylated hydroxylysines prevents the intracellular tetramerization of type VI collagen and leads to impaired secretion of type IV and VI collagens.
Lysyl hydroxylase 3 (LH3) modifies proteins in the extracellular space, a novel mechanism for matrix remodeling
Theextracellular localization and the ability of LH3 to modify lysyl residues of extracellular proteins in their native, nondenaturated conformation reveals a new dynamic in extracllular matrix remodeling, suggesting a novel mechanism for adjusting the amount of hydroxylysine and hydroXYlysine‐linked carbohydrates in collagenous proteins.
Serum chemokine levels in major depressive disorder