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J Biol Chem, Vol. 274, Issue 51, 36083-36088, December 17, 1999
From the Laboratory of Physical and Structural Biology, NICHD,
National Institutes of Health, Bethesda, Maryland 20892
Over the last several decades, it has been
established that proteolytic removal of short, non-helical terminal
peptides (telopeptides) from type I collagen significantly alters the
kinetics of in vitro fibrillogenesis. However, it has also
been observed that the protein is still capable of forming fibers even
after complete removal of telopeptides. This study focuses on the
characterization of this fibrillogenesis competency of collagen. We
have combined traditional kinetic and thermodynamic assays of
fibrillogenesis efficacy with direct measurements of interaction
between collagen molecules in fibers by osmotic stress and x-ray
diffraction. We found that telopeptide cleavage by pepsin or by up to
20 h of Pronase treatment altered fiber assembly kinetics, but the
same fraction of the protein still assembled into fibers. Small-angle x-ray diffraction showed that these fibers have normal, native-like D-stagger. Force measurements indicated that collagen-collagen interactions in fibers were not affected by either pepsin or Pronase treatment. In contrast, prolonged (>20 h) Pronase treatment resulted in cleavage of the triple helical domain as indicated by
SDS-polyacrylamide gel electrophoresis. The triple-helix cleavage
correlated with the observed decrease in the fraction of protein
capable of forming fibers and with the measured loss of attraction
between helices in fibers. These data suggest that telopeptides play a
catalytic role, whereas the information necessary for proper molecular
recognition and fiber assembly is encoded in the triple helical domain
of collagen.
Does the Triple Helical Domain of Type I Collagen Encode
Molecular Recognition and Fiber Assembly while Telopeptides Serve as
Catalytic Domains?
EFFECT OF PROTEOLYTIC CLEAVAGE ON FIBRILLOGENESIS AND ON
COLLAGEN-COLLAGEN INTERACTION IN FIBERS*
and
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
On leave from the Engelhardt Inst. of Molecular Biology, Russian
Academy of Sciences, Moscow, Russia.
§
To whom correspondence should be addressed: LPSB/NICHD, NIH, Bldg.
12A, Rm. 2041, Bethesda, MD 20892. Fax: -301-496-2172; E-mail:
leikin@helix.nih.gov.
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