The hemostatic activity of Manilkara zapota (L.) P. Royen latex associated with fibrinogenolytic activity
DOI:
https://doi.org/10.14719/pst.2020.7.3.775Keywords:
Manilkara zapota, Fibrinogenolytic, Procoagulant, Serine proteaseAbstract
Manilkara zapota (L.) P. Royen (Sapotaceae), is widely used in traditional medicine for various ailments like, diarrhea, pulmonary diseases, piles, ulcers and to treat wounds. The present study evaluates the role of M. zapota latex in hemostasis. The processed latex named as M. zapota natant latex (MzNL), has proteins at the concentration of 8 mg/ml and showed protein bands in Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The proteolytic activity of MzNL was evaluated using casein in comparison with trypsin. The phenylmethylsulfonyl fluoride (PMSF) inhibited the protease activity indicating the possible presence of serine protease. The effect of temperature, pH and metal ions on proteolytic activity was evaluated. MzNL exhibited fibrinogenolytic activity by hydrolysing A? and B? subunits of fibrinogen. However, ? subunit remained resistant for hydrolysis. MzNL hydrolyzed all the subunits of collagen type I and IV at the concentration of 8 µg and 25 µg in 20 µl each respectively. MzNL showed procoagulant activity and is devoid of hemolytic activity. Fibrinogenolytic activity and procoagulant nature of MzNL suggests its possible role in blood coagulation that in turn restores hemostasis.
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Periayah MH, Halim AS, Saad AZM. Mechanism action of platelets and crucial blood coagulation pathways in hemostasis. Int J Hematol Oncol Stem Cell Res. 2017;11(4):319–27.
Costa JO, Fonseca KC, Garrote-Filho MS, Cunha CC, Freitas MV, Silva H.S, et al. Structural and functional comparison of proteolytic enzymes from plant latex and snake venoms. Biochimie. 2010;92:1760–65. https://doi.org/10.1016/j.biochi.2010.09.002
Gubbiveeranna V, Kusuma CG, Bhavana S, Sumachirayu CK, Ravikumar H, Nagaraju S. Potent procoagulant and platelet aggregation inducing serine protease from Tridax procumbens extract. Pharmacogn Res. 2019;1:363–70. https://doi.org/ 10.4103/pr.pr_4_19
Raju EV, Divakar G. An overview on microbial fibrinolytic proteases. Int J Pharm Sci Res. 2013;5:643–56. https://doi.org/10.13040/IJPSR.0975-8232
Uday P, Achar RR, Poojitha BR, Rinimol VR, Bindu J, Nafeesa Z, et al. Laticiferous plant proteases in wound care. Int J Pharm Pharm Sci. 2015;7:44–49.
Venkatesha SH, Rajaiah R, Vishwanayh BS. Hemostatic interference of plant latex proteases. SM J Clin Pathol. 2016;1:1002.
Shivaprasad HV, Riyaz M, Venkatesh KR, Dharmappa KK, Tarannum S, Siddesha JM, et al. Cysteine proteases from the Asclepiadaceae plants’ latex exhibited thrombin and plasmin like activities. J Thromb Thrombolysis. 2009;28:304–08. https://doi.org/10.1007/s11239-008-0290-2
Bashir S. Pharmacological importance of Manilkara zapota and its bioactive constituents. Latinoam Caribe Plant Med Aromat. 2019;18:347–58. https://doi.org/10.35588/blacpma.19.18.4.22
Bano M, Ahmed B. Manilkara zapota (L.) P. Royen (Sapodilla): A review. Int J Adv Res Ideas Innov Technol. 2017;3:1364–71.
Shafii ZA, Basri M, Malek EA, Ismail M. Phytochemical and antioxidant properties of Manilkara zapota (L.) P. Royen fruit extracts and its formulation for cosmeceutical application. Asian J Plant Sci Res. 2017;7:29–41. https://doi.org/10.5685/plmorphol.29.41
Kwan. The plant observatory. Online; 2008 January 26 [cited 2020 Jun 7]. Available from: www.natureloveyou.sg
Reyes-Gomez S, Montiel R, Tlenkopatchev MA. Chicle gum from Sapodilla (Manilkara zapota) as a renewable resource for metathesis transformations. J Mex Chem Soc. 2018;61(1). https://doi.org/10.29356/jmcs.v62i1.581
Ma J, Luo XD, Protiva P, Yang H, Ma C, Basile MJ, et al. Bioactive novel polyphenols from the fruit of Manilkara zapota (Sapodilla). J Nat Prod. 2003;66:983–86. https://doi.org/10.1021/np020576x
Jadhav SS. Sapota a wonderful fruit from nature: A review. Int J Food Sci Nutr. 2018;3:1–4.
Swarnakumari S, Periyanayagam K, Ida-christi VE, Mohan S. Phytochemical screening and in-vitro corneal wound healing activity of the leaves of Manilkara zapota (L.) P. Royen var. Pkm1 in newer herbal drug development. World J Pharm Res. 2017;6:639–47. https://doi.org/10.20959/wjpr20179-9224
Satake K, Okuyama T, Ohashi M, Shinoda T. The spectrophotometric determination of amine, amino acid and peptide with 2,4,6?trinitrobenzene1?sulfonic acid. J Biochem. 1960;47:654–60. https://doi.org/10.1111/j.1949-8594.1960.tb08465.x
Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227:680–85. https://doi.org/10.1038/228549a0
Leach BS, Collawn JF, Fish WW. Behavior of glycopolypeptides with empirical molecular weight estimation methods. 2. In random coil producing solvents. Biochemistry. 1980;19:5741–47. https://doi.org/10.1021/bi00566a012
Condrea E, Yang CC, Rosenberg P. Anti-coagulant activity and plasma phosphatidylserine hydrolysis by snake venom phospholipases A2. Thromb Haemost. 1983;49(2):151. htttps://doi.org/10.1055/s-0038-1657347
Kim M, Hamilton S, Guddat L, Overall CM. Plant collagenase: Unique collagenolytic activity of cysteine proteases from ginger. Biochim Biophys Acta. 2008;1770:1627–35. https://doi.org/10.1016/j.bbagen.2007.08.003
Shin SY, Lee MK, Kim KL, Hahm KS. Structure-antitumor and hemolytic activity relationships of synthetic peptides derived from cecropin A-magainin2 and cecropin A-melittin hybrid peptides. J Peptidr Rrs. 1997;50:279–85. https://doi.org/10.1111/j.1399-3011.1997.tb01469.x
Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the folin phenol reagent. J Biol Chem. 1951;193:265–75. https://doi.org/10.1016/0304-3894(92)87011-4
Raskovic BG, Polovic ND. Collegenase activity in fig latex could contribute to its efficacy in ethnomedicinal preparations. J Herb Med. 2016;6:73–78. http://dx.doi.org/doi:10.1016/j.hermed.2016.03.002
Rajesh R, Shivaprasad HV, Raghavendra GCD, Nataraju A, Dhananjaya BL, Vishwanath BS. Comparative study on plant latex proteases and their involvement in hemostasis: A special emphasis on clot inducing and dissolving properties. Planta Med. 2007;73:1061–67. https://doi.org/10.1055/s-2007-981575
Viana CA, Oliveira JS, Freitas CDT, Alencar NMN, Carvalho CPS, Nishi BC, et al. Thrombin and plasmin– like activities in the latices of Cryptostegia grandiflora and Plumeria rubra. Blood Coagul Fibrinolysis. 2013;24:386–92. https://doi.org/10.1097/MBC.0b013e32835d540b
Badgujar SB. Evaluation of hemostatic activity of latex from three Euphorbiaceae species. J Ethnopharmacol. 2014;151:733–39. http://dx.doi.org/10.1016/j.jep.2013.11.044
Shivaprasad HV, Rajaiah R, Frey BM. Frey FJ, Vishwanath BS. 'Pergularain e I'- a plant cysteine protease with thrombin-like activity from Pergularia extensa latex. Thromb Res. 2010;125:100–05. https://doi.org/10.1016/j.thromres.2009.10.002
Patel GK, Kawale AA, Sharma AK. Purification and physicochemical characterization of a serine protease with fibrinolytic activity from latex of a medicinal herb Euphorbia hirta. Plant Physiol Biochem. 2012;52:104–11. https://doi.org/10.1016/j.plaphy.2011.12.004
Uday P, Maheshwari M, Sharanappa P, Nafeesa Z, Kameshwar VH, Priya BS, et al. Exploring hemostatic and thrombolytic potential of heynein - A cysteine protease from Ervatamia heyneana latex. J Ethnopharmacol. 2017;199:316–22. https://doi.org/10.1016/j.jep.2016.12.047
Frye KE, Luterman A. Decreased incidence of hypertrophic burn scar formation with the use of collagenase, an enzymatic debriding agent. Wounds. 2005;17:332–36.
Hurst LC, Badalamente MA, Hentz VR, Hotchkiss RN, Kaplan FT, Meals RA, et al Injectable collagenase Clostridium histolyticum for dupuytren's contracture. N Engl J Med. 2009;361:968–79. https://doi.org/10.1056/NEJMoa0810866
Onesti MG, Fioramonti P, Carella S, Fino P, Sorvillo V, Scuderi N. A new association between hyaluronic acid and collagenase in wound repair: an open study. Eur Rev Med Pharmacol Sci. 2013;17:210–16.
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Copyright (c) 2020 C G Kusuma, Vinod Gubbiveeranna, C K Sumachirayu, S Bhavana, H Ravikumar, S Nagaraju
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