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inhibition of collagen, and thrombin-induced platelet aggregation by lansberg's hognose pit viper (porthidium lansbergii hutmanni) venom.the porthidium genus is represented by the p. lansbergii rozei and p. lansbergii hutmanni (plh) subspecies in venezuela. the venom components of these have been little studied, probably due to the low incidence of reported accidents, although acute and serious local effects such as invasive edema and disseminated ecchymosis are present during human envenonation. the aim of this work was to characterize the in vitro effects of crude p. l. hutmanni venom, and its fractions, on platelet aggregation ...200717486300
inhibition of the hemorrhagic and proteolytic activities of lansberg's hognose pit viper (porthidium lansbergii hutmanni) venom by opossum (didelphis marsupialis) serum: isolation of didelphis marsupialis 0.15dm fraction on deae-cellulose chromatography.earlier studies have revealed the ability of sera from several mammals to neutralize the toxic effects of snake venom. the venezuelan opossum (didelphis marsupialis) is one that has been found to inhibit hemorrhagic and proteolytic activities of venoms from many species of snakes. in this article it is shown that the opossum sera and its 0.15dm fraction were able to completely neutralize both hemorrhagic and hydrolysis (proteolysis) of casein effects induced by venom of the lansberg's hognose pi ...200818800269
inhibition of adrenaline and adenosine diphosphate induced platelet aggregation by lansberg's hognose pit viper (porthidium lansbergii hutmanni) venom.the haemostatic components of venom from the genus porthidium has been poorly studied, although it is known that severe manifestations occur when humans are envenomed, which include invasive oedema and disseminated ecchymosis. the effects of venom on blood platelets are commonly studied and are normally carried out with platelet-rich plasma (prp). a series of crude venom dilutions was used to determine the effects of adenosine diphosphate (2 microm) and adrenaline (11 microm) induced platelet ag ...200717891398
divergent functional profiles of acidic and basic phospholipases a2 in the venom of the snake porthidium lansbergii lansbergii.the lansberg's hognose pitviper, porthidium lansbergii lansbergii, inhabits northern colombia. a recent proteomic characterization of its venom (j. proteomics [2015] 114, 287-299) revealed the presence of phospholipases a2 (pla2) accounting for 16.2% of its proteins. the two most abundant pla2s were biochemically and functionally characterized. pllans-i is a basic, dimeric enzyme with a monomer mass of 14,136 da, while pllans-ii is an acidic, monomeric enzyme of 13,901 da. both have asp49 in the ...201627381371
proteomic and functional analyses of the venom of porthidium lansbergii lansbergii (lansberg's hognose viper) from the atlantic department of colombia.the venom of the lansberg's hognose pitviper, porthidium lansbergii lansbergii, a species found in the northern region of colombia, is poorly known. aiming to increase knowledge on porthidium species venoms, its proteomic analysis and functional evaluation of in vitro and in vivo activities relevant to its toxicity were undertaken. out of 51 protein components resolved by a combination of rp-hplc and sds-page, 47 were assigned to 12 known protein families. in similarity with two previously chara ...201525496801
purification and characterization of a metalloproteinase, porthidin-1, from the venom of lansberg's hog-nosed pitvipers (porthidium lansbergii hutmanni).porthidium lansbergii hutmanni is a small pit viper found on margarita island, venezuela. local tissue damage is one of the most obvious characteristics of p. l. hutmanni envenomation, which can lead to diverse pathological effects, such as hemorrhage, edema, blistering, necrosis, lymphatic vessel damage and degradation of extracellular matrix. metalloproteinases are one of the major components in venoms responsible for these effects. to date, very little is known or has been reported on p. l. h ...201121255600
antitumoral potential of lansbermin-i, a novel disintegrin from porthidium lansbergii lansbergii venom on breast cancer cells.disintegrins from snake venoms bind with high specificity cell surface integrins, which are important pharmacological targets associated with cancer development and progression.201931385773
phylogeny and toxicological assessments of two porthidium lansbergii lansbergii morphotypes from the caribbean region of colombia.after a snakebite accident, species identification is of vital importance. however, the existence of intraspecific differences in the body coloration patterns of venomous snakes can generate confusion and delay a convenient and effective treatment. this is the situation for porthidium lansbergii lansbergii from colombia, for which two distinctive color morphs occur, and the relationship of these morphs with venom toxicity is unknown. therefore, venom samples from specimens of these two morphs we ...201931129160
antitumor potential of pllans-ii, an acidic asp49-pla2 from porthidium lansbergii lansbergii snake venom on human cervical carcinoma hela cells. 201930218735
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