Structures physiological regulation

JL Madara, JR Pappenheimer. Structural basis for physiological regulation of para-cellular pathways in intestinal epithelia. J Membrane Biol 100 149-164, 1987. 

Nagatsu I. (1995). Tyrosine hydroxylase human isoforms, structure and regulation in physiology and pathology. Essays Biochem. 30, 15-35. 

Another factor that can influence the distribution of therapeutic peptides and proteins is binding to endogenous protein structures. Physiologically active endogenous peptides and proteins frequently interact with specific binding proteins involved in their transport and regulation. 

J. L. Madaira and I. R. Fappenhdracr. Structural basis for physiological regulation of paraoellular pathways In intestinal epithella. 7. Mmhr. BioL 100 149 (1987). 

A correlation of enhanced synthesis of polyamines with rapid growth or cell proliferation has been observed 21. From a physiological point of view, polyamines are implicated as regulators of cell proliferative activity 22). It is well known that polyamines, as protonated polycations, can bind with nucleotide and nucleic acid anions 23 241 to affect biochemical reactivities and stabilize tertiary structures 25,26). 

The Ca2+-binding subunit TN-C is homologous to calmodulin with four EF-hands. In contrast to calmodulin, which is ubiquitously expressed in multicellular eukaryotic organisms and interacts with many targets, troponin specifically regulates muscle contraction. There are some structural differences between Troponin C in skeletal and cardiac muscles reflecting their physiological differences. 

Nonmuscle/smooth muscle myosins-Il are structurally similar to striated muscle myosin-II, but they have slower rates of ATP hydrolysis than do their striated muscle counterparts. Nonmuscle/smooth muscle myosin-II is also regulated differently than striated muscle myosin-II. Nonmuscle myosin-II is divided into the invertebrate and vertebrate branches (Cheney et al., 1993). This group is ubiquitous because it is present in most lower organisms, such as slime molds, amoeba, sea urchins, etc., and in virtually all mammalian nonmuscle cells. Smooth muscle myosin-II is also somewhat heterogeneous in that at least three separate forms of smooth muscle heavy chains, with molecular weights of 196,000, 200,000, and 204,000 have been identified (Kawamoto and Adelstein, 1987). The physiological properties of these separate myosin heavy chains are not yet known. 

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