Lecture 4 Cell-Matrix Interactions 2 - MitchellThom , structureintheECM o

Lecture 4 Cell-Matrix Interactions 2 - MitchellThom ,...

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Cell Physiology Lecture 4 September 16 2013 Cell Matrix Interactions II Mitchell Thom - Collagen is one of many components of the ECM, and it is the most abundant  structure in the ECM - The alpha helix of Collagen is called the  collagen fibril.   o The amino acids that are in the middle of the helix are Glycines. o o A usual repeating sequence is Glycine- Proline- Hydroxyproline o The N and C-terminus are globular domains that help to wind the trimer  together - Over 20 different types of Collagen o All 3 proteins in the repeating sequence of collagen can differ to create  different collagens. o Remember that collagens can also be homo or heterodimers depending on  if the individual components are from the same gene or not - - Collagens 1 2 3 are the common ones o In the ER the polypeptide chains are hydroxylated and then glycosylated o Proline and Lysine are the ones that are usually hydroxylated  Not all prolines and lysines! Hydroxylated lysines are glycosylated o Scurvy= lack of vitamin C leading to weak collagen Collagen cannot be hydroxylated without vitamin C How does hydroxylation lead to collagen integrity? o An oligosaccharide (multiple sugars) is added to the N-terminus in the  Golgi o The globular domains at the N and C terminus are cleaved out of the cell  where the fibrils then cross link (Fibrillogenesis) to form the ECM  suprastructure - Collagen VI o Multimer, not a trimer o Globular domains are not removed as they are a component of the  tropocollagen structure Therefore some collagens need the N and C globular domains to be removed, while some require them to function - Differences Between Collagen Types - Number of helix repeat: ie. The length of the triple helix portion
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  • Fall '09
  • Golgi Apparatus, Collagen, Glycosaminoglycan, collagens

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