Collagen hydrolysate intake increases skin collagen expression and suppresses matrix metalloproteinase 2 activity

J Med Food. 2011 Jun;14(6):618-24. doi: 10.1089/jmf.2010.0085. Epub 2011 Apr 11.


The effect of daily ingestion of collagen hydrolysate (CH) on skin extracellular matrix proteins was investigated. Four-week-old male Wistar rats were fed a modified AIN-93 diet containing 12% casein as the reference group or CH as the treatment group. A control group was established in which animals were fed a non-protein-modified AIN-93 diet. The diets were administered continuously for 4 weeks when six fresh skin samples from each group were assembled and subjected to extraction of protein. Type I and IV collagens were studied by immunoblot, and activities of matrix metalloproteinase (MMP) 2 and 9 were assessed by zymography. The relative amount of type I and IV collagens was significantly (P < .05) increased after CH intake compared with the reference diet group (casein). Moreover, CH uptake significantly decreased both proenzyme and active forms of MMP2 compared with casein and control groups (P < .05). In contrast, CH ingestion did not influence on MMP9 activity. These results suggest that CH may reduce aging-related changes of the extracellular matrix by stimulating anabolic processes in skin tissue.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Collagen / administration & dosage*
  • Collagen / chemistry
  • Collagen / genetics*
  • Collagen / metabolism
  • Dietary Supplements / analysis
  • Down-Regulation / drug effects*
  • Humans
  • Male
  • Matrix Metalloproteinase 2 / genetics
  • Matrix Metalloproteinase 2 / metabolism*
  • Protein Hydrolysates / administration & dosage*
  • Protein Hydrolysates / chemistry
  • Rats
  • Rats, Wistar
  • Skin / drug effects
  • Skin / enzymology*
  • Skin / metabolism
  • Skin / physiopathology
  • Skin Aging / drug effects*
  • Skin Aging / genetics


  • Protein Hydrolysates
  • Collagen
  • Matrix Metalloproteinase 2