Developmental Changes in the Late Larva of Calliphora Stygia Iv. Uptake of Plasma Protein by the Fat Body

Martín, M. M.; Kinnear, Judith F; Thomson, J.E.

doi:10.1071/bi9710291

Cited by 52 publications

(16 citation statements)

References 17 publications

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“…From the feeding to wandering stages, an increase in the concentration of the proteins represented by bands F15-19 takes place. With the exception of F19, further increase in the concentration of these proteins in quiescent larvae is probably due not to de novo protein synthesis, but rather to uptake of these proteins from the haemolymph (Martin, Kinnear, and Thomson 1971). The decrease in total plasma protein which occurs during mid and late third instar (Kinnear et al 1968) supports this view.…”

Section: (I) Proteins Of Fat Body and Plasmasupporting

confidence: 70%

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Developmental Changes in the Late Larva of Calliphora Stygia Iii. The Occurrence and Synthesis of Specific Tissue Proteins

Kinnear¹,

Martín²,

Thomson³

1971

Aust. Jnl. Of Bio. Sci.

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The occurrence and synthesis of soluble proteins from certain larval tissues of O. 8tygia have been examined by acrylamide.gel electrophoresis and autoradiography at the feeding (days 4-6), wandering (days 7-10), and quiescent (day 11) stages of third-instar development. The protein species investigated are distributed as follows: fat body, 22; plasma, 21; body wall, 18; salivary gland cells, 16; salivary secretion, 18.The predominant soluble proteins of fat body, body wall, and salivary gland cells are in each case synthesized in situ. All ma.jor plasma proteins are synthesized in the fat body and are electrophoretically comparable with those released by the fat body in vitro. Most of the proteins of the salivary secretion are synthesized by the gland cells: the main secretory species are not derived directly from the haemolymph. A minimum of 40,25, and 45% respectively of the soluble species detectable in extracts of fat body, body wall, and salivary gland cells are specific to these tissues.Individual protein species fall into three contrasting groups according to whether their synthesis occurs: (1) in the feeding stage only; (2) in post-feeding stages only; (3) throughout third instar.In each tissue an abrupt and coordinated reduction in protein synthesis takes place at the end of the feeding stage. Unidentified, presumably humoral, regulatory agents appear likely to be responsible. The synthesis of certain specific proteins is differentially affected by these controlling influences.

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Section: (I) Proteins Of Fat Body and Plasmasupporting

confidence: 70%

“…By the wandering and quiescent stages, the amount of soluble protein in the fat body increases [ Fig. 3(a); see also Martin, Kinnear, and Thomson 1971]. This is mainly seen in bands F15-19, but is also evident in bands F4-10.…”

Section: (A) Plasmamentioning

confidence: 77%

Developmental Changes in the Late Larva of Calliphora Stygia Iii. The Occurrence and Synthesis of Specific Tissue Proteins

Kinnear¹,

Martín²,

Thomson³

1971

Aust. Jnl. Of Bio. Sci.

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“…At the end of larval life hexamerins are cleared in part from the haemolymph by the larval fat-body cells (e.g., Martin et al, 1971 ;Ueno and Natori, 1982;Marinotti and de Bianchi, 1986;Burmester and Scheller, 1992). Specific hexamerin receptors have been reported in the dipteran C. vicina Scheller, 1992, 1995a) and S. peregrina (Ueno and Natori, 1984), and in the lepitopteran Helicoverpa zea (Wang and Haunerland, 1994 b).…”

Section: Discussionmentioning

confidence: 99%

Conservation of Hexamerin Endocytosis in Diptera

Burmester

Scheller

1997

European Journal of Biochemistry

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In cyclorrhaphan Diptera at least two different types of haemolymph proteins exist which belong to the class of hexamerins. In the last larval instar of Calliphora vicina, the highly aromatic hexamerin, arylphorin, and the second hexamerin, PII, make up about 90% of haeniolymph proteins. Both of these proteins are selectively taken up by the fat body cells at the end of larval life and share a common membrane-bound receptor. In addition, hexamerins and possible hexamerin receptors of Calliphora vicina, Calliphora vomitoria, Drosophila melanogaster, Ceratitis capitata, Sarcophaga bullata, Musca domestica and Protophormia terraenovae were investigated. Uptake of arylphorin by the larval fat bodies of Calliphoru vicina as well asarylphorin-receptor binding can be competed in vitro by haemolymph from other Diptera. Therefore, hexamerin-receptor binding must be conserved among related cyclorrhaphan Diptera and between different types of hexamerins within a species. As the degree of competition is in good agreement with the presumed phylogenetic distances between these species, the method described here provides a simple tool to estimate evolutionary distances.

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“…The protein is synthe sized in the larval fat body and secreted into the hemolymph, where it accumulates (82,85). At the conclusion of the fe eding period, synthesis stops and reabsorption takes place from the hemolymph into the fa t body concurrently with the appearance of dense protein granules in the fa t body cells (87); at adult emergence, only 0.03 mg of soluble plasma calliphorin per individual remains. When 14C-Iabeled calliphorin was administered to late larvae, 14C02 was released during adult development and adult proteins were labeled (89).…”

Section: Storage Proteinsmentioning

confidence: 99%