Formation of Arrowhead Complexes with Heavy Meromyosin in a Variety of Cell Types

نویسندگان

  • Harunori Ishikawa
  • Richard Bischoff
  • Howard Holtzer
چکیده

Heavy meromyosin (HMM) forms characteristic arrowhead complexes with actin filaments in situ. These complexes are readily visualized in sectioned muscle. Following HMM treatment similar complexes appear in sectioned fibroblasts, chondrogenic cells, nerve cells, and several types of epithelial cells. Thin filaments freshly isolated from chondrogenic cells also bind HMM and form arrowhead structures in negatively stained preparations. HMM-filament complexes are prominent in the cortex of a variety of normal metaphase and Colcemid-arrested metaphase cells. There is no detectable binding of HMM with other cellular components such as microtubules, 100-A filaments, tonofilaments, membranes, nuclei, or collagen fibrils. The significance of HMM-filament binding is discussed in view of the finding that arrowhead complexes form in types of cells not usually thought to contain actin filaments.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Growth cones make proteins, too

Actin in nonmuscle cells n the late 1960s, Howard Holtzer’s group at the University of Pennsylvania made the unexpected observation that virtually all eukaryotic cells assemble a variety of actinbased structures (Ishikawa et al., 1969). At that time, scientists thought that actin and myosin were restricted to muscle cells and ascribed contractile activity in other cells to a variety of molecule...

متن کامل

Actin in nonmuscle cells

Actin in nonmuscle cells n the late 1960s, Howard Holtzer’s group at the University of Pennsylvania made the unexpected observation that virtually all eukaryotic cells assemble a variety of actinbased structures (Ishikawa et al., 1969). At that time, scientists thought that actin and myosin were restricted to muscle cells and ascribed contractile activity in other cells to a variety of molecule...

متن کامل

N-ethylmaleimide-modified heavy meromyosin. A probe for actomyosin interactions

Treatment of rabbit skeletal muscle heavy meromyosin (HMM) with the sulfhydryl reagent N-ethylmaleimide (NEM) produces a species of HMM which remains tightly bound to actin in the presence of MgATP. NEM-HMM forms characteristic "arrowhead" complexes with actin which persist despite rinses with MgATP. NEM-HMM inhibits the actin activation of native HMM-ATPase activity, the superprecipitation of ...

متن کامل

MICROFILAMENTS IN CHAOS CAROLINENSIS Sand Heavy Meromyosin Binding in the Glycerinated Cell

Recent ultrastructural studies indicate that 50-70 A microfilaments are found in a variety of cell types (1, 10, 25, 27), some of which exhibit shape changes (6, 26), cell motility (4, 5, 17, 18), and cytoplasmic streaming (2, 3, 28) . Biochemical investigators have isolated and purified an actinlike protein from Physarum polycephalum (2, 29-33), the amoebae of Dictyostelium discoideum (34), an...

متن کامل

Electron Microscopic Investigations of Actomyosin as a Function of Ionic Strength

Natural actomyosin at micro = 0.6 appears in various forms, including the regular arrowhead structures originally reported by Huxley (1), when it has been stained negatively with 1% uranyl acetate. In addition to the arrowheads, thin whiskers, 700-1200 A in length and 20 A in width, attached to the arm of the arrowheads have been demonstrated. The dimensions of the whiskers and arms of the arro...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Journal of Cell Biology

دوره 43  شماره 

صفحات  -

تاریخ انتشار 1969