Type XXIV Collagen

Signe Holm Nielsen; Morten Asser Karsdal

doi:10.1016/B978-0-12-809847-9.00024-6

Type XXIV Collagen

Signe Holm Nielsen, Morten Asser Karsdal

Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review

Abstract

Type XXIV collagen is a fibrillar collagen containing two collagenous domains and three noncollagenous domains. The amino-terminal peptide contains a thrombospondin N-terminal–like motif and a highly charged segment interspersed with several tyrosine residues. Type XXIV collagen is predominately expressed in the formation of bone; however, it has recently been found in the brain, muscle, kidney, spleen, liver, lung, testis, and ovary, but to a far lesser extent than in bone. COL24A1 is increased during squamous cell carcinoma of the head and neck and could be a marker of osteoblast differentiation and certain types of cancers. Currently there are no mutations in humans or mice associated with biological functions, and no biomarkers have been put forward.

Original language	English
Title of host publication	Biochemistry of Collagens, Laminins and Elastin : Structure, Function and Biomarkers
Publisher	ScienceDirect
Publication date	2016
Pages	143-145
Chapter	24
ISBN (Print)	978-0-12-809847-9
DOIs	https://doi.org/10.1016/B978-0-12-809847-9.00024-6
Publication status	Published - 2016
Externally published	Yes

Access to Document

10.1016/B978-0-12-809847-9.00024-6

Fingerprint Dive into the research topics of 'Type XXIV Collagen'. Together they form a unique fingerprint.

Cite this

@inbook{5b4fcc0411ae4b7db03f411eabea3966,

title = "Type XXIV Collagen",

abstract = "Type XXIV collagen is a fibrillar collagen containing two collagenous domains and three noncollagenous domains. The amino-terminal peptide contains a thrombospondin N-terminal–like motif and a highly charged segment interspersed with several tyrosine residues. Type XXIV collagen is predominately expressed in the formation of bone; however, it has recently been found in the brain, muscle, kidney, spleen, liver, lung, testis, and ovary, but to a far lesser extent than in bone. COL24A1 is increased during squamous cell carcinoma of the head and neck and could be a marker of osteoblast differentiation and certain types of cancers. Currently there are no mutations in humans or mice associated with biological functions, and no biomarkers have been put forward.",

author = "Nielsen, {Signe Holm} and Karsdal, {Morten Asser}",

year = "2016",

doi = "10.1016/B978-0-12-809847-9.00024-6",

language = "English",

isbn = "978-0-12-809847-9",

pages = "143--145",

booktitle = "Biochemistry of Collagens, Laminins and Elastin",

publisher = "ScienceDirect",

}

TY - CHAP

T1 - Type XXIV Collagen

AU - Nielsen, Signe Holm

AU - Karsdal, Morten Asser

PY - 2016

Y1 - 2016

N2 - Type XXIV collagen is a fibrillar collagen containing two collagenous domains and three noncollagenous domains. The amino-terminal peptide contains a thrombospondin N-terminal–like motif and a highly charged segment interspersed with several tyrosine residues. Type XXIV collagen is predominately expressed in the formation of bone; however, it has recently been found in the brain, muscle, kidney, spleen, liver, lung, testis, and ovary, but to a far lesser extent than in bone. COL24A1 is increased during squamous cell carcinoma of the head and neck and could be a marker of osteoblast differentiation and certain types of cancers. Currently there are no mutations in humans or mice associated with biological functions, and no biomarkers have been put forward.

AB - Type XXIV collagen is a fibrillar collagen containing two collagenous domains and three noncollagenous domains. The amino-terminal peptide contains a thrombospondin N-terminal–like motif and a highly charged segment interspersed with several tyrosine residues. Type XXIV collagen is predominately expressed in the formation of bone; however, it has recently been found in the brain, muscle, kidney, spleen, liver, lung, testis, and ovary, but to a far lesser extent than in bone. COL24A1 is increased during squamous cell carcinoma of the head and neck and could be a marker of osteoblast differentiation and certain types of cancers. Currently there are no mutations in humans or mice associated with biological functions, and no biomarkers have been put forward.

U2 - 10.1016/B978-0-12-809847-9.00024-6

DO - 10.1016/B978-0-12-809847-9.00024-6

M3 - Book chapter

SN - 978-0-12-809847-9

SP - 143

EP - 145

BT - Biochemistry of Collagens, Laminins and Elastin

PB - ScienceDirect

ER -