On the Third Active Peptide on Smooth Muscle in the Skin of Rana nigromaculata HALLOWELL

1968 ◽  
Vol 16 (10) ◽  
pp. 2088-2089 ◽  
Author(s):  
TERUMI NAKAJIMA
Keyword(s):  
Smooth Muscle ◽  
Active Peptide ◽  
The Third ◽  
Rana Nigromaculata

scholarly journals The studies on the active peptide on smooth muscle in the skin of Rana rugosa, Thr6-bradykinin and its analogous peptide, ranakinin-R.

1979 ◽  
Vol 27 (2) ◽  
pp. 486-491 ◽  
Author(s):  
TADASHI YASUHARA ◽  
OSAMU ISHIKAWA ◽  
TERUMI NAKAJIMA ◽  
KENGO ARAKI ◽  
SHINRO TACHIBANA
Keyword(s):  
Smooth Muscle ◽  
Active Peptide

scholarly journals Production of the third and fourth component of complement (C3, C4) by smooth muscle cells

Immunology ◽  
1996 ◽  
Vol 89 (2) ◽  
pp. 183-188 ◽  
Author(s):  
Y. UEDA ◽  
K. NAGASAWA ◽  
H. TSUKAMOTO ◽  
T. HORIUCHI ◽  
H. NISHIZAKA ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Muscle Cells ◽  
Complement C3 ◽  
The Third ◽  
Fourth Component

Bronchoprotective effect of simulated deep inspirations in tracheal smooth muscle

2014 ◽  
Vol 117 (12) ◽  
pp. 1502-1513 ◽  
Author(s):  
Christopher D. Pascoe ◽  
Graham M. Donovan ◽  
Ynuk Bossé ◽  
Chun Y. Seow ◽  
Peter D. Paré
Keyword(s):  
Smooth Muscle ◽  
Lung Function ◽  
Airway Smooth Muscle ◽  
Forced Expiratory Volume ◽  
Airway Responsiveness ◽  
Tracheal Smooth Muscle ◽  
Airway Wall ◽  
Methacholine Challenge ◽  
Airway Narrowing ◽  
The Third

Deep inspirations (DIs) taken before an inhaled challenge with a spasmogen limit airway responsiveness in nonasthmatic subjects. This phenomenon is called bronchoprotection and is severely impaired in asthmatic subjects. The ability of DIs to prevent a decrease in forced expiratory volume in 1 s (FEV1) was initially attributed to inhibition of airway narrowing. However, DIs taken before methacholine challenge limit airway responsiveness only when a test of lung function requiring a DI is used (FEV1). Therefore, it has been suggested that prior DIs enhance the compliance of the airways or airway smooth muscle (ASM). This would increase the strain the airway wall undergoes during the subsequent DI, which is part of the FEV1 maneuver. To investigate this phenomenon, we used ovine tracheal smooth muscle strips that were subjected to shortening elicited by acetylcholine with or without prior strain mimicking two DIs. The compliance of the shortened strip was then measured in response to a stress mimicking one DI. Our results show that the presence of “DIs” before acetylcholine-induced shortening resulted in 11% greater relengthening in response to the third DI, compared with the prior DIs. This effect, although small, is shown to be potentially important for the reopening of closed airways. The effect of prior DIs was abolished by the adaptation of ASM to either shorter or longer lengths or to a low baseline tone. These results suggest that DIs confer bronchoprotection because they increase the compliance of ASM, which, consequently, promotes greater strain from subsequent DI and fosters the reopening of closed airways.

scholarly journals A filamentous cytoskeleton in vertebrate smooth muscle fibers.

1976 ◽  
Vol 68 (3) ◽  
pp. 539-556 ◽  
Author(s):  
P Cooke
Keyword(s):  
Molecular Weight ◽  
Smooth Muscle ◽  
Muscle Protein ◽  
Muscle Fibers ◽  
Thin Filaments ◽  
The Third ◽  
Dense Bodies ◽  
Thick Filaments ◽  
Myosin Filaments ◽  
Cell Fractions

There are three classes of myofilaments in vertebrate smooth muscle fibers. The thin filaments correspond to actin and the thick filaments are identified with myosin. The third class of myofilaments (100 A diam) is distinguished from both the actin and the myosin on the basis of fine structure, solubility, and pattern of localization in the muscle fibers. Direct structural evidence is presented to show that the 100A filament constitute an integrated filamentous network with the dense bodies in the sarcoplasm, and that they are not connected to either the actin or myosin filaments. Examination of (a) isolated dense bodies, (b) series of consecutive sections through the dense bodies, and (c) redistributed dense bodies in stretched muscle fibers supports this conclusion. It follows that the 100-A filaments complexes constitute a structrally distinct filamentous network. Analysis of polyacrylamide gels after electrophoresis of cell fractions that are enriched with respect to the 100-A filaments shows the presence of a new muscle protein with a molecular weight of 55,000. This protein can form filamentous segments that closely resemble in structure the native, isolated 100-A filaments. The results indicate that the filamentous network has a structure and composition that distinguish it from the actin and myosin in vertebrate smooth muscle.

scholarly journals ISOLATION OF A FRAGMENT (C3a) OF THE THIRD COMPONENT OF HUMAN COMPLEMENT CONTAINING ANAPHYLATOXIN AND CHEMOTACTIC ACTIVITY AND DESCRIPTION OF AN ANAPHYLATOXIN INACTIVATOR OF HUMAN SERUM

1969 ◽  
Vol 129 (5) ◽  
pp. 1109-1130 ◽  
Author(s):  
Viktor A. Bokisch ◽  
Hans J. Müller-Eberhard ◽  
Charles G. Cochrane
Keyword(s):  
Smooth Muscle ◽  
Human Serum ◽  
Enzymatic Reaction ◽  
Disc Electrophoresis ◽  
Chemotactic Activity ◽  
Small Fragment ◽  
Human Complement ◽  
The Third ◽  
Biologic Activity ◽  
Basic Portion

A small fragment of C3, called C3a, which has smooth muscle contracting activity, was isolated by three different methods. At pH 8.6, C3a behaved as cation, and using the Archibald method, its mol wt was determined to be 7000. A specific antiserum to C3a showed the fragment to be antigenically distinct from the rest of the C3 molecule, i.e., the C3b portion. The same antiserum and an anti-whole C3 were able to inhibit the biologic activity of C3a. In addition to anaphylatoxin activity, leukocyte chemotactic activity was shown to reside in C3a. Treatment with trypsin caused the cationic fragment to become anionic and abolished the anaphylatoxin but not the chemotactic activity. C3a fragments with identical biologic activity and comparable cationic properties, as determined by acid disc electrophoresis, were obtained by treatment of C3 with C3 convertase, C3 inactivator complex, trypsin, and plasmin. Thrombin produced a similar C3 fragment which was inactive. It was concluded that C3a corresponds to an unusually basic portion of C3 which may be liberated by attack of a variety of enzymes on a highly susceptible region of the native C3 molecule. C3b was cleaved by trypsin and less efficiently by thrombin or plasmin into two antigenically distinct pieces: the larger C3c fragment corresponding to ß1A and the smaller C3d fragment to α2D of aged serum. The c- and the d-fragments were separated and characterized. Isolated C3a rapidly lost its anaphylatoxin activity when treated with small amounts of a partially purified, thermolabile 10S α-pseudoglobulin of human serum. The conditions of inactivation suggested an enzymatic reaction. The anaphylatoxin inactivator also destroyed the activity of C5-derived anaphylatoxin and of lysyl bradykinin.

scholarly journals Isolation and Structure of a New Active Peptide "Xenopsin"on the Smooth Muscle, especially on a Strip of Fundus from a Rat Stomach, from the Skin of Xenopus laevis

1973 ◽  
Vol 21 (12) ◽  
pp. 2801-2804 ◽  
Author(s):  
KENGO ARAKI ◽  
SHINRO TACHIBANA ◽  
MIKIO UCHIYAMA ◽  
TERUMI NAKAJIMA ◽  
TADASHI YASUHARA
Keyword(s):  
Smooth Muscle ◽  
Xenopus Laevis ◽  
Rat Stomach ◽  
Active Peptide

scholarly journals Re: Whither smooth muscle antibodies in the third millennium?

2002 ◽  
Vol 55 (7) ◽  
pp. 558-559
Author(s):  
S J Katona ◽  
P C Cooper ◽  
M E Cramp ◽  
E R Kaminski
Keyword(s):  
Smooth Muscle ◽  
The Third ◽  
Third Millennium ◽  
Smooth Muscle Antibodies
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