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Ascorbic acid-dependent collagen formation in penaeid shrimp.

B Hunter1, P C Magarelli, D V Lightner

  • 1University of Arizona, Environmental Research Laboratory, Tucson 85706.

Comparative Biochemistry and Physiology. B, Comparative Biochemistry
|January 1, 1979
PubMed
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Black death in shrimp is linked to underhydroxylated collagen. Ascorbic acid (AsA) is crucial for proline hydroxylation in collagen formation, impacting shrimp health and disease resistance.

Area of Science:

  • Aquatic animal health
  • Biochemistry
  • Marine biology

Background:

  • Black death is an ascorbic acid (AsA) deficiency disease affecting penaeid shrimp.
  • Collagen is a vital structural protein, and its proper formation is essential for tissue integrity.

Purpose of the Study:

  • To investigate the link between black death disease in shrimp and collagen underhydroxylation.
  • To determine the role of ascorbic acid in collagen synthesis and proline hydroxylation in penaeid shrimp.

Main Methods:

  • Quantified collagen as hydroxyproline (HYP) in Penaeus californiensis and P. stylirostris across various body weights.
  • Assessed prolyl hydroxylase (PH) activity in shrimp tissues using radiolabeled proline.
  • Conducted nutritional trials to evaluate the dietary requirement of AsA for collagen formation.

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Main Results:

  • Established a logarithmic relationship between total body collagen HYP and body weight (y = 90x1.18).
  • Identified tissues prone to mechanical stress (subcutis, hindgut, gills) as having higher HYP levels and being more susceptible to AsA deficiency.
  • Demonstrated AsA-dependent prolyl hydroxylase activity essential for proline hydroxylation in shrimp collagen synthesis.

Conclusions:

  • Shrimp collagen underhydroxylation is associated with black death disease.
  • Ascorbic acid is indispensable for prolyl hydroxylase activity and collagen proline hydroxylation in penaeid shrimp.
  • Dietary AsA is critical for maintaining collagen integrity and preventing disease in shrimp.