Isolation and protein pattern of eye lens fiber junctions

Dunia, I.; Ghosh, Chayanjit; Benedetti, E.L.

doi:10.1016/0014-5793(74)80831-8

Cited by 82 publications

(15 citation statements)

References 14 publications

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“…This assumption is probably consistent with the morphological features of fiber junctions and with our recent observation that those structural complexes, isolated by detergent solubilization, display a rather simple protein pattern characterized by a major constituent of 34,000 daltons (12).…”

Section: It Is Noteworthy That Streams Of Inner Membrane Particlessupporting

confidence: 90%

“…In contrast to many other developing tissues, the lens is composed of one type of epithelium which during the entire life of the animal will continuously, and in one direction, differentiate into lens fibers (10). Furthermore, the latter cells are extensively connected by a rather unique type of junction (11,12).We present some evidence that in the region of cellular elongation, where the epithelium loses the ability to divide and differentiates into cortical fibers, the assembly of newly formed junctions is characterized by the progressive accumulation of particles. Initially these inner membrane particles form linear rows.…”

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Development of Junctions During Differentiation of Lens Fibers

Benedetti

Dunia

Bloemendal

1974

Proc. Natl. Acad. Sci. U.S.A.

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Throughout the differentiation of eye lens epithelium into fibers, an extensive system of intercellular junctions develops. The junctional assembly is initially characterized by the accumulation of 9.0-nm intramombranous particles, forming linear rows in the matching plasma membranes of adjoining fibers. At the final stage of the fiber differentiation, the junctional particles are assembled in geometrically packed arrays.The formation of linear rows and bidiniensional lattices of intramembranous particles probably favors reciprocal recognition of cell surfaces and specific cell-to-cell inter. locking. Moreover, the existence of a rather rigid lipid core of the plasma membrane of eye lens fiber may promote the clustered distribution of intramembranous particles and facilitate the junctional assembly.In. almost all animal tissues, low-resistance passageways and metabolic cooperation correlate with the presence of "gap" junctions (1-3). Freeze-fracturing has revealed that this type of junction is characterized by arrays of repeating particles associated with the inner hydrophobic matrix of the junctional membranes. Moreover, the arrays of particles are interlocked by a hexagonal lattice of pitted facets, likely originating from the merging of both outer membrane leaflets (4, 5). Although many membrane-mediated functions, such as fusion (6) and interaction of cell surface receptors with specific ligands (7), have been tentatively correlated with the spatial rearrangement and perturbation of the inner membrane particles made visible by freeze-fracturing, circumstantial evidence illustrating the differentiation of plasma membranes during cell contact and assembly of low-resistance junctions is still incomplete.Some data have been already presented illustrating the junctional features in embryonic and developing tissues (8,9). From these interesting studies it is, however, not easily apparent whether some plasma membrane aspects identified in freeze-fracturing experiments represent the assembly of "gap" junctions or stages of its breakdown and dilution during organogenesis and tissue differentiation. In the present study, the development of intercellular junctions in the eye lens is investigated. The vertebrate lens has several unique features that make this avascular tissue particularly suitable for the analysis of differentiation processes. In contrast to many other developing tissues, the lens is composed of one type of epithelium which during the entire life of the animal will continuously, and in one direction, differentiate into lens fibers (10). Furthermore, the latter cells are extensively connected by a rather unique type of junction (11,12).We present some evidence that in the region of cellular elongation, where the epithelium loses the ability to divide and differentiates into cortical fibers, the assembly of newly formed junctions is characterized by the progressive accumulation of particles. Initially these inner membrane particles form linear rows. Later they assemble in geometrically packed arra...

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Section: It Is Noteworthy That Streams Of Inner Membrane Particlessupporting

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Development of Junctions During Differentiation of Lens Fibers

Benedetti

Dunia

Bloemendal

1974

Proc. Natl. Acad. Sci. U.S.A.

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“…We have shown [3] that lens fiber junctions, purified by detergent solubilization and sucrose gradient centrifugation, are characterized by the two major components MP26 and MP34. Freeze fracture experiments show that the differentiation of the communicating junctions existing between elongating and terminally differentiated fibers is characterized by an accumulation of intramembranous particles of protein nature ( fig.3).…”

Section: Iandsands and Discussionmentioning

confidence: 99%

Changes in membrane protein pattern in relation to lens cell differentiation

et al. 1977

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“…Goodenough (1) was first to isolate a junctional protein from liver and later coined the word "connexin" to describe this component (2). Since then, there has been a proliferation of the number of polypeptides that were suspected to be part of the gap junction structure (3)(4)(5)(6)(7)(8). Most of the previously published work has relied on the morphological appearance of the fractions as a single criterion to estimate the purity and intactness of the gap junction preparations used for analysis.…”

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Independent lines of evidence suggesting a major gap junctional protein with a molecular weight of 26,000.

Finbow¹,

Yancey²,

Johnson³

et al. 1980

Proc. Natl. Acad. Sci. U.S.A.

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Several polypeptides have been described in the past as components of gap junction fractions. Of these, a peptide of Mr 26,000 is found in gap junctions isolated from livers of different species under conditions that minimize proteolysis. Tryptic digestion of purified "intact" junctions causes the rapid disappearance of this peptide with a concomitant appearance of a band of Mr 10,000, which has previously been found to be characteristic of junctional fractions isolated with the aid of proteolytic treatment. Both the peptides of Mr 26,000 and 10,000 are missing from gap junction preparations after partial hepatectomy, when gap junctions are absent from the surface of the hepatocytes. They have reappeared in fractions from the livers of animals killed 3 days postoperatively, when gap junctions are again present in vivo.

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Isolation and protein pattern of eye lens fiber junctions

Cited by 82 publications

References 14 publications

Development of Junctions During Differentiation of Lens Fibers

Development of Junctions During Differentiation of Lens Fibers

Changes in membrane protein pattern in relation to lens cell differentiation

Independent lines of evidence suggesting a major gap junctional protein with a molecular weight of 26,000.

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