Books > Medicine > Pre-clinical medicine: basic sciences > Anatomy > Cytology
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Myosin - Biosynthesis, Classes and Function (Paperback)
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Myosin - Biosynthesis, Classes and Function (Paperback)
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Myosin: Biosynthesis, Classes and Function opens with a discussion
on class I myosins, the most varied members of the myosin
superfamily and a remarkable group of molecular motor proteins that
move actin filaments and produce force. Class I myosin molecules
have various physiological roles including maintenance of normal
intestinal brush border structure, glucose homeostasis, glomerular
filtration, immune function, and tumor promotion and suppression,
and new studies are revealing that mutations may lead to diseases
including cancer and kidney disease. Thus, the authors review the
structure and function of the eight myosin-I isoforms (Myo1a-Myo1h)
that are expressed in mammals. Next, the book discusses muscle
contractile function and its association with the activity of the
protein complex actomyosin, in which myosin exhibits enzyme
activity, namely the ability to hydrolyze ATP. The demonstrated
ability of calix[4]arenes C-97, C-99, C-90 and thiacalix[4]arenes
C-798 and C-800 can be used for further research aimed at the use
of these compounds as novel pharmacological agents able to
efficiently restore normal contractile function of myometrium by
inhibition or activation of this function, or the eliminating
negative effects of heavy metal cations. Following this, the
authors present the results of their experiments on studying the
effects of different isotopes of magnesium and zinc on the
enzymatic activity of myosin, namely the catalytic subfragment-1 of
myosin, isolated from myometrium muscle. It has been revealed that
the rate of the enzymatic ATP hydrolysis is 22.5 times higher in
the reaction media enriched with the magnetic isotope, 25Mg, as
compared to the activity of the same enzyme in the reaction media
enriched with the nonmagnetic isotopes, 24Mg or 26Mg or MgCl2 of
natural isotope abundance. Continuing, precipitation/extraction
methods and MALDI TOF/TOF mass spectrometry were used in order to
and identify, for the first time, a protein with the molecular mass
of 48 kDa as a fragment of human unconventional myosin 1c isoform b
in a blood serum of multiple sclerosis patients. Western-blot
analysis using commercial monospecific anti-human Myo1c antibodies
has shown that the molecular mass of this protein obtained from a
blood serum of different human sources varied in between 46-48 kDa.
Thus, the authors name the 46-48 kDa proteins revealed in a blood
serum as a short form of the human unconventional myosin 1c (sMyo
1C).
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