Study of catheptic and acid phosphatase activities during development and metamorphosis ofDrosophila melanogaster

Mulherkar, Leela; Kothari, R. M.; Vaidya, V. G.

doi:10.1007/bf00582006

Cited by 10 publications

(4 citation statements)

References 11 publications

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“…Essentially, the same pattern of degeneration has been found in other organisms during the metamorphosis, i.e., whole larvae of Drosophila (Mulherkar et al 1972), larval organ in insect such as salivary gland (Price 1974;Lockshin and Williams 1965) and amphibian tadpole (Robinson 1972;Hourdry 1974). Modes of the acid phosphatase activity observed in whole larvae in the present work are consistent with those of these authors.…”

Section: Discussionsupporting

confidence: 92%

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FINE STRUCTURAL AND BIOCHEMICAL STUDIES ON CELL DEATH OF THE DEVELOPING BAR EYE DISCS IN DROSOPHILA MELANOGASTER

Michinomae

1976

The Japanese journal of genetics

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Section: Discussionsupporting

confidence: 92%

“…In insects, cell death is generally observed in the destruction of larval tissues during metamorphosis, and attending to an increase in hydrolytic enzyme activity (Lockshin and Williams 1965;Mulherkar et al 1972;Henrikson and Clever 1972).…”

mentioning

confidence: 99%

FINE STRUCTURAL AND BIOCHEMICAL STUDIES ON CELL DEATH OF THE DEVELOPING BAR EYE DISCS IN DROSOPHILA MELANOGASTER

Michinomae

1976

The Japanese journal of genetics

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“…This process of activation is catalyzed by (a) phosphorylation of their serine/theonine residues at –OH groups (Itoh, 2000), (b) transglutaminase (Tgase) action (Sporn et al, 1987), (c) glucosidases for modification (Moroco et al, 1997), (d) proteolytic reduction in MW, (e) breaking hydrogen bonds in acidic pH, (f) exposure to higher temperature and (g) treatment with urea (Blumenfeld and Livne, 1999). Proteolytic enzymes, plasmin, MMPs II/III (D'Angelo et al, 2001; Maeda et al, 2001), cathepsin B (Mulherkar et al, 1972), alkaline and acid proteases (Shah et al, 1986; Ramamurthy et al, 1991) activate latent TGF‐β in vitro. Ability of the cells to activate latent TGF‐β is a critical regulatory step in its in vivo action.…”

Section: Transformation Of Inactive Isoforms To Active Formsmentioning

confidence: 99%

An update on transforming growth factor-β (TGF-β): Sources, types, functions and clinical applicability for cartilage/bone healing

2011

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Transforming growth factor-β (TGF-β) has been reviewed for its sources, types of isoforms, biochemical effects on cartilage formation/repair, and its possible clinical applications. Purification of three isoforms (TGF-β-1, β-2 and β-3) and their biochemical characterization revealed mainly their homo-dimer nature, with heterodimers in traces, each monomer comprised of 112 amino acids and MW. of 12 500 Da. While histo-chemical staining by a variety of dyes has revealed precise localization of TGF-β in tissues, immune-blot technique has thrown light on their expression as a function of age (neonatal vs. adult), as also on its quantum in an active and latent state. X-ray crystallographic studies and nuclear magnetic resonance (NMR) analysis have unraveled mysteries of their three-dimensional structures, essential for understanding their functions. Their similarities have led to interchangeability in assays, while differences have led to their specialized clinical applicability. For this purpose, their latent (inactive) form is changed to an active form through enzymatic processes of phosphorylation/glycosylation/transamination/proteolytic degradation. Their functions encompass differentiation and de-differentiation of chondrocytes, synthesis of collagen and proteoglycans (PGs) and thereby maintain homeostasis of cartilage in several degenerative diseases and repair through cell cycle signaling and physiological control. While several factors affecting their performance are already identified, their interplay and chronology of sequences of functions is yet to be understood. For its success in clinical applications, challenges in judicious dealing with the factors and their interplay need to be understood.

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“…During autophagic degradation of tissues, some enzymatic functions such as acid phosphatase change according to degree of the cell death process. Therefore their activities and localization have been studied during insect metamorphosis (Mulherkar et al 1972;Csikós & Sass 1998;Ianella et al 2008). In the present study, acid phosphatase activity is demonstrated as an indicator of autophagic cell death.…”

Section: Effects On Acid Phosphatasementioning

confidence: 99%

Fenoxycarb modulates ecdysone receptor B1 and programmed cell death of the anterior silk gland of silkworm Bombyx mori

Göncü

Parlak

2011

Entomological Science

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Fenoxycarb, carbamate has been shown to be one of the most potent juvenile hormone analogues against a variety of insect species. In the present study, topical application of fenoxycarb to fifth-instar larvae of the silkworm Bombyx mori (Lepidoptera: Bombycidae) was performed immediately after the fourth ecdysis (on day 0), day 3 and day 6 of the instar and then its effects on the anterior silk glands (ASG) and ecdysone receptor B1 (EcR-B1) protein were investigated during larval pupal development. Fenoxycarb application increased the instar length and prevented metamorphic events, depending on the application time. The ASGs of B. mori undergo programmed cell death during the larval-pupal metamorphosis and an insect steroid, 20-hydroxyecdysone (20E), triggers this cell death. The exact mechanism by which 20E and juvenile hormone regulates programmed cell death in insect tissues is poorly understood. To gain insights into how juvenile hormone regulates metamorphic events like programmed cell death in the anterior silk glands, we analyzed the progression of programmed cell death with morphological observations and biochemical experiments like acid phosphatase activity and DNA electrophoresis. Then we examined the EcR-B1 protein levels and their relationships with programmed cell death. Our results indicated that fenoxycarb modulates programmed cell death of the anterior silk glands and EcR-B1 protein level, depending on the application time. Fenoxycarb may exhibit its effects in at least two different ways: (i) acting on prothoracic gland secretory activity; and/or (ii) regulation of EcR-B1 expression in the anterior silk glands for programmed cell death process.

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Study of catheptic and acid phosphatase activities during development and metamorphosis ofDrosophila melanogaster

Cited by 10 publications

References 11 publications

FINE STRUCTURAL AND BIOCHEMICAL STUDIES ON CELL DEATH OF THE DEVELOPING <i>BAR</i> EYE DISCS IN <i>DROSOPHILA MELANOGASTER</i>

FINE STRUCTURAL AND BIOCHEMICAL STUDIES ON CELL DEATH OF THE DEVELOPING <i>BAR</i> EYE DISCS IN <i>DROSOPHILA MELANOGASTER</i>

An update on transforming growth factor-β (TGF-β): Sources, types, functions and clinical applicability for cartilage/bone healing

Fenoxycarb modulates ecdysone receptor B1 and programmed cell death of the anterior silk gland of silkworm Bombyx mori

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