Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 3 de 3
Filter
Add more filters










Database
Language
Publication year range
1.
Biol Bull ; 186(3): 309-18, 1994 Jun.
Article in English | MEDLINE | ID: mdl-8043656

ABSTRACT

The actions of FMRFamide-related peptides (FaRPs) on the neurogenic heart of the horseshoe crab, Limulus polyphemus, were investigated. Excitatory chronotropic effects were produced by application of TNRNFLRFamide, SDRNFLRFamide, GYNRS-FLRFamide, or pQDPFLRFamide to the intact heart preparation. Effects were dose-dependent with a threshold of 10(-9) M or less. TNRNFLRFamide and SDRNFLRFamide increased the burst rate of the isolated Limulus cardiac ganglion. Synthetic FaRPs produced inotropic excitation of the heartbeat as well. GYNRSFLRFamide, TNRNFLRFamide, SDRNFLRFamide, and pQDPFLRFamide increased heart contraction strength at a threshold dose of approximately 10(-8) M. TNRNFLRFamide and SDRNFLRFamide enhanced electrically evoked contractions of the Limulus myocardium, elicited contracture in some preparations, and increased the excitability of cardiac muscle fibers. The presence of cardioactive FaRPs in the Limulus central nervous system was suggested by reverse phase HPLC of acidified methanol extracts of Limulus nervous tissue. Four peaks of FaRP-like bioactivity were detected with the Busycon radula protractor muscle bioassay. These peaks also contained FaRP-like immunoreactivity. Two of these partially purified peaks produced excitatory chronotropic effects on the intact Limulus heart preparation similar to those produced by synthetic FaRPs.


Subject(s)
Horseshoe Crabs/drug effects , Invertebrate Hormones/pharmacology , Neuropeptides/pharmacology , Amino Acid Sequence , Animals , FMRFamide , Ganglia, Invertebrate/drug effects , Ganglia, Invertebrate/physiology , Heart/drug effects , Heart/physiology , Heart Rate/drug effects , Horseshoe Crabs/physiology , Molecular Sequence Data , Myocardial Contraction/drug effects , Stimulation, Chemical
2.
Philos Trans R Soc Lond B Biol Sci ; 340(1291): 25-38, 1993 Apr 29.
Article in English | MEDLINE | ID: mdl-8099743

ABSTRACT

Major ampullate (MaA) and minor ampullate (MiA) silk glands of juvenile Araneus cavaticus (third to penultimate instars) were examined by dissection at various times relative to ecdysis. Several days before ecdysis the larger pairs of MaA and MiA glands become non-functional and remain so until ecdysis. Nevertheless, proecdysial spiders are able to draw ampullate fibres due to the presence of smaller pairs of MaA and MiA glands which are functional at this time. Indeed, it appears that these smaller ampullate glands are intended for use only during proecdysis. Thus, larger MaA and MiA glands and smaller MaA and MiA glands are typically not used concurrently (a brief transitional period is an exception). The smaller ampullate glands functioning in one juvenile stadium regress in the following stadium and become (what have previously been referred to as) accessory MaA and MiA glands. These nonfunctional accessory ampullate glands do not re-develop into functional smaller ampullate glands until the following stadium. Thus, a given pair of smaller MaA or MiA glands is only functional in every other juvenile stadium. However, because there are two sets of smaller/accessory MaA and MiA glands which function alternately, the spider is able to produce ampullate fibres during the proecdysial portion of each stadium. A new terminology for the larger, smaller and accessory ampullate glands is proposed which emphasizes the kinship between the two sets of smaller/accessory ampullate glands.


Subject(s)
Spiders/physiology , Animals , Female , Larva , Male , Microscopy, Electron, Scanning , Sebaceous Glands/cytology , Sebaceous Glands/physiology , Sebaceous Glands/ultrastructure , Spiders/cytology , Spiders/growth & development
3.
Peptides ; 11(2): 205-11, 1990.
Article in English | MEDLINE | ID: mdl-2356151

ABSTRACT

A proctolin-like peptide was isolated from the prosomal CNS of the chelicerate arthropod, Limulus, and purified using size exclusion, ion exchange and high performance liquid chromatography. Coincident bioassay (cockroach hindgut) and radioimmunoassay were employed to identify fractions which contained proctolin-like material. Proctolin-like activity coeluted with synthetic proctolin with all three chromatographic techniques employed. When applied to either the Limulus heart or hindgut preparations, purified Limulus proctolin produced excitatory responses which were indistinguishable from those produced by the synthetic peptide. Purified samples of the Limulus proctolin-like peptide were subjected to Edman degradation and tandem mass spectrometry and the amino acid sequence of the Limulus peptide was determined to be identical to that of cockroach proctolin (H-Arg-Tyr-Leu-Pro-Thr-OH). The presence of proctolin in the Limulus CNS and its biological action on the isolated heart and hindgut suggest a physiological role for this peptide in the regulation of cardiac output and hindgut motility.


Subject(s)
Central Nervous System/analysis , Horseshoe Crabs/analysis , Neuropeptides , Oligopeptides/isolation & purification , Amino Acid Sequence , Animals , Arthropods/physiology , Chromatography/methods , Cockroaches , Female , Intestinal Mucosa/metabolism , Male , Molecular Sequence Data , Myocardium/metabolism , Oligopeptides/physiology , Radioimmunoassay
SELECTION OF CITATIONS
SEARCH DETAIL
...