# CHEMISTRY AND BIOLOGY OF NORMAL AND ABNORMAL COLLAGENS

> **NIH NIH R01** · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · 1987 · $123,155

## Abstract

We plan to establish the complete primary structure of the remaining,
unfinished portions of 1) type II collagen from human hyaline cartilage, 2)
type V collagen from human placentae and 3) the basement
membrane-associated type IV and 7S collagens from human placentae,
including the amino acid sequence and the post-translational modifications
such as hydroxylation of prolyl and lysyl residues and glycosylation of the
hydroxylysyl residues.  This objective is a part of our long term studies
to understand the biochemical and molecular bases for the structural and
"nonstructural" functions of collagens and their alterations and roles in
various experimental and human diseases.  The foundation for the proposed
work has been carefully laid during the past grant periods by isolation and
characterization of the genetically distinct types of collagens, and the
component CNBr peptides derived from them.  The complete amino acid
sequence of Alpha 1(I), Alpha2 and Alpha1(III) has now been established.
The sequence analysis of Alpha1(V) is approximately 40% completed
(Alpha1(V)-CB1, 4 and 7 and most of CB5), and that for Alpha 2 (V) is
approximately 10% completed (Alpha2(V)-CB5 and most of CB4).  The
Alpha1(IV) chain is also approximately 30% completed (Alpha 1
(IV)-CB2,3,4,5 and 9 and partial sequences of CB6, 7 and 8).  The work on
Alpha2(IV), Alpha1(II) and 7S has been initiated.  Collagen is the most
ubiquitouxly distributed protein in the human body, and plays a critical
role in the maintenance of the architectural integrity and function of
organs.  It is intimately involved in various physiologival processes such
as m orphogenesis and tissue remodeling.  It is also involved in a vaiety
of pathologic states, some acquired and others inherited.  It is also
becoming increasingly clear that collagen and collagen-derived products
exert important biologic effects on various cells involved in inflammation;
e.g., platelets, macrophages and fibroblasts.  Detailed information on the
primary structure of this family of proteins is, therefore, essential to
our understanding of its biologic properties and behavior.

## Key facts

- **NIH application ID:** 3154914
- **Project number:** 5R01AR016506-15
- **Recipient organization:** UNIVERSITY OF TENNESSEE HEALTH SCI CTR
- **SAM.gov UEI:** X1M1PN3KG3E7
- **Principal Investigator:** ANDREW H KANG
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1987
- **Award amount:** $123,155
- **Award type:** 5
- **Project period:** 1978-04-01 → 1988-03-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3154914

## Citation

> US National Institutes of Health, RePORTER application 3154914, CHEMISTRY AND BIOLOGY OF NORMAL AND ABNORMAL COLLAGENS (5R01AR016506-15). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3154914. Licensed CC0.

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