# CHARACTERIZATION OF A NEW HUMAN COLLAGEN

> **NIH NIH R01** · OREGON HEALTH & SCIENCE UNIVERSITY · 1987 · $96,269

## Abstract

The basement membrane zones of the dermal-epidermal junction of skin and of
several other external tissues are more complex than the basement membranes
of more internal tissues.  This specialized complexity is reflected both
ultrastructurally by the presence of unique fibrous structures, and
immunologically by the presence of antigens not found in other basement
membranes.  The anchoring fibril is one of these structures.  The anchoring
fibril is a centrosymmetrically banded fiber, about 800 nm in length, whose
major structural component is Type VII collagen.  The anchoring fibril
subunit is an antiparallel linear dimer of Type VII collagen molecules
crosslinked to each other at their amino terminii through an overlap of 60
nm.  The distal ends of the anchoring fibril contains large
carboxy-terminal globular domains of this collagen type.  Each Type VII
molecule contributes a domain of approximately 450 kd.  Often these
globular domains at one end of the anchoring fibril are embedded within the
lamina densa.  Anchoring fibril can either form a horseshoe-shaped
structure with the distal end also inserting into the lamina densa, or it
can extend perpendicular to the basal lamina into the dermis with its
distal end inserted into what appears as an amorphous patch.  This
amorphous "island" contains aggregates of carboxy-terminal globular domain
of Type VII collagen, Type IV collagen, laminin and perhaps other basement
membrane components.  Additional anchoring fibrils can bridge these
islands, and are seen projecting further into the dermis, again terminating
in additional islands.  As a result, the anchoring fibrils form an extended
network 1-1/2 to 2 Mu into the dermis.  We propose to examine the
intermolecular interactions responsible for the formation and stabilization
of this network, by identifying and quantitating these interactions at the
molecular level.  This will be done by isolating reactive fragments from
the interacting components, determining the amino acid sequence of the
interactive regions, and relating these to the amino acid sequence fo the
carboxy-terminal globular domain of Type VII collagen.  An analysis of this
extended network of anchoring fibrils within the subbasal lamina of
patients with recessive-dystrophic Epidermolysis Bullosa will help to
determine the function of this network as well as contribute to our
understanding of the molecular pathology of this disease condition.

## Key facts

- **NIH application ID:** 3157240
- **Project number:** 5R01AR035532-04
- **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:** 1987
- **Award amount:** $96,269
- **Award type:** 5
- **Project period:** 1984-09-01 → 1989-08-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3157240

## Citation

> US National Institutes of Health, RePORTER application 3157240, CHARACTERIZATION OF A NEW HUMAN COLLAGEN (5R01AR035532-04). Retrieved via MORVS 2026-10-24 from https://api.morvs.ai/grant/nih/3157240. Licensed CC0.

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