Target intelligence / Profile preview

Collagen type XIX alpha 1 chain (COL19A1)

Target
COL19A1
Molecular classification
Fibril-associated collagen with interrupted triple helices (FACIT collagen), Structural protein, Extracellular matrix protein
01

Overview

Collagen type XIX alpha 1 chain (COL19A1) is a structural protein encoded by the COL19A1 gene, classified as a fibril-associated collagen with interrupted triple helices (FACIT). It assembles as a homotrimer of three alpha-1 chains and is mainly located in basement membranes of various tissues, including muscle, heart, and the central nervous system. Type XIX collagen is most abundant in embryonic and early postnatal tissues, particularly skeletal muscle and certain neurons, and is critical for proper muscle differentiation and extracellular matrix architecture[1][2][5]. Its protein domains allow interaction and cross-bridging between collagen fibrils and other ECM molecules, helping regulate tissue organization and repair[1][2][4]. The NC1 domain of the protein can be cleaved to generate fragments (matricryptins) with reported anti-tumor and anti-angiogenic properties. Altered expression of COL19A1 is associated with disease states: in amyotrophic lateral sclerosis, increased COL19A1 expression in muscle and blood reflects degeneration and may act as a compensatory mechanism, making it a promising biomarker for disease progression. It may also modulate extracellular matrix in the heart and is linked to certain muscular and connective tissue disorders[1][2][5]. There are no known drugs targeting COL19A1 directly, nor established clinical use as a therapeutic target, but its role in tissue remodeling and disease processes is a subject of ongoing research.

Other names
Collagen alpha-1(XIX) chainCollagen alpha-1(Y) chainCOL9A1LD6S228Ea1 chain of type XIX collagencollagen XIX, alpha-1 polypeptidecollagen alpha 1 (Y) chaincollagen, type XIX, alpha 1
02

Biological functions

Maintenance of extracellular matrix integrity and stability[1][5]Modulation of collagen fibril formation, cross-linking, and organization, especially in heart and muscle[2][4]Structural support in basement membranes[1]Involvement in muscle differentiation, maturation, and possibly neuron function[1][4]Modulation of cell migration, adhesion, proliferation, differentiation, and chemotaxis[1]
03

Disease associations

Neurodegenerative disease (notably amyotrophic lateral sclerosis/ALS as prognostic biomarker and potential therapeutic target)[1]Cancer (anti-tumor and anti-angiogenic effects via NC1 domain-derived fragments)[1]Heart disease (implicated in cardiac structure and ECM organization, though not as a direct cause)[2]Muscular and connective tissue diseases (e.g., Megaesophagus, Ullrich congenital muscular dystrophy 1A)[5]Other
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Safety considerations

No direct safety concerns or known pharmacological liabilities reported. Therapeutic targeting not established; potential challenge is tissue specificity and unknown systemic impacts.
05

Biomarkers

Prognostic biomarker for ALS progression and functional state[1]Possible biomarker for muscle or neurodegenerative tissue integrity

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