COL12A1

Last update 08 May 2025

Basic Info

Synonyms

COL12A1, COL12A1L, Collagen alpha-1(XII) chain

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Introduction

Type XII collagen interacts with type I collagen-containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix.

100 Clinical Results associated with COL12A1

100 Translational Medicine associated with COL12A1

0 Patents (Medical) associated with COL12A1

240

Literatures (Medical) associated with COL12A1

01 Jun 2025·Poultry Science

Spatial transcriptomic differences in the breast muscle of grower broilers at 21 and 28 days of age

Article

Author: Bowker, Brian ; Zhuang, Hong ; Gudidoddi, Seshidhar Reddy ; Goo, Doyun ; Choppa, Venkata Sesha Reddy ; Han, Gippeum ; Shakeri, Majid ; Lee, Jihwan ; Kong, Byungwhi ; Choi, Janghan ; Kim, Woo Kyun

This study investigated transcriptomic differences between the caudal and cranial areas in breast muscle in the grower phase of broiler chickens (D 21 and D 28). A total of 66 one-day-old broiler chickens were allotted to 6 cage pens of 11 birds per pen. On D 21 and D 28, one bird per pen was randomly selected, and breast muscle samples were collected in the caudal and cranial areas of the Pectoralis major. RNA sequencing was conducted, followed by screening for differentially expressed genes (DEGs; P < 0.05) and multivariate analyses. A total of 24,498 genes were identified, and 8,831 genes had greater than 100 mean read count. On D 21, there were 666 DEGs, among which 482 and 184 genes were down-regulated and up-regulated, respectively, in the caudal area compared with the cranial area. There were 2 down-regulated and 56 up-regulated genes with a greater than 1.5-fold change (FC). On D 28, there were 872 DEGs, among which 408 and 464 genes were down-regulated and up-regulated, respectively. There were 12 down-regulated and 23 up-regulated genes with a greater than 1.5-fold change. Principal component analysis (PCA) plots showed that gene profiles were not distinctly separated between the caudal area and the cranial area of breast muscle on D 21 and D 28. On D 21, collagen type XI alpha 1 chain (COL11A1), fibromodulin (FMOD), myosin heavy chain 7B (MYH7B), carbonic anhydrase 3A (CA3A), tenomodulin (TNMD), COL12A1, carboxypeptidase Z (CPZ), lysyl oxidase like 2 (LOXL2), COL1A1, and COL1A2 were significantly down-regulated in the caudal area compared to the cranial area with a greater than 2-FC (P < 0.05). KEGG pathway enrichment analysis indicated that various pathways including regulation of actin cytoskeleton, ribosome, and focal adhesion were significantly different in the caudal area compared with the cranial area. These findings suggest that spatial differences in gene expression within the breast muscle could be linked to functional or developmental variations between regions, potentially influencing muscle growth, meat quality, and breast myopathies. Understanding these spatial transcriptomic differences may provide insights into identifying etiologies and developing strategies for breast myopathies.

01 Apr 2025·Biochemical and Biophysical Research Communications

Collagen XII deficiency promotes ligament-specific heterotopic ossification via fibrochondrocyte differentiation

Article

Author: Okada, Yukina ; Hiyama, Sakura ; Sugidono, Akira ; Kajikawa, Shuhei ; Fukunaga, Yuko ; Yoneda, Taiju ; Fujihara, Kei ; Izu, Yayoi ; Koch, Manuel

Heterotopic ossification of tendons and ligaments causes pain and dysfunction, significantly reducing quality of life. However, its underlying mechanisms remain elusive. In addition to injury, tissue organization and stiffness have been implicated in heterotopic ossification. Collagen XII, a member of the fibril-associated collagens with interrupted triple helices (FACIT) family, plays a crucial role in maintaining the structural integrity and function of tendons and ligaments. Its deficiency alters tissue stiffness and predisposes ligaments to rupture. In this study, we investigated whether collagen XII contributes to the development of heterotopic ossification. Three-dimensional microcomputed tomography (3D-μCT) and X-ray analyses revealed heterotopic bone formation in the knee and ankle ligaments, but not in tendons, of Col12a1-deficient mice, with a 100 % incidence in mice older than 19 weeks. Histological analysis showed the presence of Alcian blue- and Toluidine blue-positive fibrochondrocyte-like cells in Col12a1-deficient ligaments, which were subsequently replaced by bone tissue, as indicated by Alizarin red staining. Real-time qPCR analysis of knee ligaments demonstrated a slight increase in chondrogenic markers and a significant upregulation of osteogenic markers in Col12a1-deficient mice compared with wild-type controls. In vitro chondrogenesis and osteogenesis assays using primary tenocytes from wild-type and Col12a1-deficient mice revealed that collagen XII deficiency enhanced osteogenic potential, whereas chondrogenic potential remained comparable. Our findings indicate that collagen XII deficiency specifically induces heterotopic bone formation in knee and ankle ligaments, occurring via fibrochondrocytes rather than through endochondral or intramembranous ossification.

01 Apr 2025·Molecular & Cellular Proteomics

Proteome-wide Investigation of Proline Hydroxylation in Pancreatic Ductal Adenocarcinoma Using DiLeu Isobaric Labeling Strategy

Article

Author: Wu, Feixuan ; Li, Lingjun ; Wang, Danqing ; Odorico, Jon S ; Tabang, Dylan Nicholas

Pancreatic ductal adenocarcinoma (PDAC) is a highly aggressive malignancy characterized by a dense fibrotic stroma intertwined with a collagen-rich extracellular matrix (ECM), which significantly contributes to tumor progression. In this study, we developed a high-throughput quantitative method that integrates enhanced hydrophilic interaction liquid chromatography (HILIC) with modified elution conditions and 12-plex N,N-dimethyl leucine (DiLeu) isobaric tags, facilitating efficient multiplexed quantitative analysis of hydroxyproline. This approach was applied to human pancreatic samples and resulted in the identification of 194 hydroxyproline peptides from 157 hydroxyproline sites and 59 proline-hydroxylated proteins, representing the first and the largest hydroxyproline proteomics dataset reported for the pancreas to date. This dataset lays a molecular foundation for understanding the structure-function relationships of hydroxyproline-containing proteins and their roles in pancreatic physiology and pathology. We then apply this strategy to investigating proline hydroxylation alterations in benign pancreatic tumors, PDAC and their normal adjacent tissues (NAT). Our findings suggest significant biological functions related to proline hydroxylation, including altered patterns of key proteins such as collagen alpha-1(I) chain and collagen alpha-1(XII) chain. These proteins emerge as potential targets for further studies on proline hydroxylation in PDAC, potentially elucidating its role in modifying protein structures and influencing cancer progression.

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COL12A1

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