# CHARACTERIZATION OF A NEW HUMAN COLLAGEN

> **NIH NIH R01** · OREGON HEALTH & SCIENCE UNIVERSITY · 1989 · $99,351

## Abstract

Type VII collagen has been characterized in this laboratory as a unique
extracellular matrix macromolecule that forms antiparallel dimers that
then aggregate laterally to form structures known as anchoring fibrils.
We have postulated that dimer formation is mediated by the amino-
terminal non-helical domain (NC-2).  The morphology of the anchoring
fibrils suggest that they may stabilize the attachment of external
epithelia to their underlying stromal matrix.  This concept is
strengthened by the finding that individuals with the disease of
recessive dystropic Epidermolysis Bullosa, characterized by spontaneous
separation of the epithelia from the stroma through the plane of the
anchoring fibrils, lack both identifiable anchoring fibrils and type VII
collagen.

One consequence of the antiparallel arrangement of type VII collagen and
the subsequent lateral aggregation is that the two ends of the anchoring
fibril are identical.  These ends, containing the carboxy-termininal
non-helical domain (NC-1), interact with the epithelial basement
membrane and with structures we described as "anchoring plaques" that
are aggregates of the NC-1 domains, type IV collagen and perhaps other
intrinsic basement membrane components.  These spatial relationships
suggest that the NC-1 domains mediate the formation and stability of the
anchoring fibril network.
Since disruptions in the anchoring fibril network have severe
pathological consequences, it is important to understand the molecular
basis for the interactions of anchoring fibrils with anchoring plaques
and with basement membranes.  We propose to characterize the structure
of type VII collagen in sufficient detail to evaluate he relationship of
its structure to its anchoring function.  We will determine the amino
acid sequence of selected portions of the molecule using conventional
biochemical methods and recombinent DNA approaches.  We will isolate and
identify subdomains of NC-1 and evaluate their secondary structure by
biophysical techniques.  Similarly, we will determine the primary
structure of NC-2.  Monoclonal antibodies made to synthetic peptides
that mimick NC-2 structure will be used to test the hypothesis that NC-2
directs type VII dimerization.  We believe that knowledge of the
detailed structure of type VII collagen will lead to the formation of an
hypothesis of how specific structural regions contribute to the
anchoring function of the macromolecule.

## Key facts

- **NIH application ID:** 3157239
- **Project number:** 2R01AR035532-06
- **Recipient organization:** OREGON HEALTH & SCIENCE UNIVERSITY
- **SAM.gov UEI:** NPSNT86JKN51
- **Principal Investigator:** ROBERT E BURGESON
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1989
- **Award amount:** $99,351
- **Award type:** 2
- **Project period:** 1984-09-01 → 1992-08-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3157239

## Citation

> US National Institutes of Health, RePORTER application 3157239, CHARACTERIZATION OF A NEW HUMAN COLLAGEN (2R01AR035532-06). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3157239. Licensed CC0.

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