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Discussion of all aspects of biological molecules, biochemical processes and laboratory procedures in the field.

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Postby blazing » Tue Oct 18, 2011 6:53 am

Can the 4-hyydroxyproline measure insoluble crosslink collagen content in heart tissue?
Last edited by JackBean on Tue Oct 18, 2011 7:02 am, edited 1 time in total.
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Postby HerrBiologie » Sun Oct 30, 2011 9:12 am

Advanced age, independent of concurrent cardiovascular disease, can be associated with increased extracellular matrix (ECM) fibrillar collagen content and abnormal diastolic function. However, the mechanisms causing this left ventricular (LV) remodeling remain incompletely defined.

We hypothesized that one determinant of age-dependent remodeling is a change in the extent to which newly synthesized procollagen is processed into mature collagen fibrils. We further hypothesized that secreted protein acidic and rich in cysteine (SPARC) plays a key role in the changes in post-synthetic procollagen processing that occur in the aged myocardium.

Young (3 mo old) and old (18–24 mo old) wild-type (WT) and SPARC-null mice were studied. LV collagen content was measured histologically by collagen volume fraction, collagen composition was measured by hydroxyproline assay as soluble collagen (1 M NaCl extractable) versus insoluble collagen (mature cross-linked), and collagen morphological structure was examined by scanning electron microscopy.
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Postby thematrix » Fri Dec 23, 2011 2:30 pm

Insoluble cross-linked collagen can be measured by determination of the 4-hydroxyproline upon hydrolysis. There are now a few commercially available kits (Biovision and Quickzyme) to quantify the hydroxyproline or measure total collagen including acid hydrolysis protocol (quickzyme)
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