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10. Clinical characteristics of women captured by extending the definition of severe postpartum haemorrhage with 'refractoriness to treatment': a cohort study

Author

Henriquez, D., Gillissen, A., Smith, S.M., Cramer, R.A., van den Akker, T., Zwart, J.J. (Joost), van Roosmalen, J.J., Bloemenkamp, KW, Bom, J.G., Adriaanse, H.J., van den Akker, E.S.A., Baas, M.I., Bank, C.M.C., Beek, E. van, de Boer, B.A.G., Boer, K. (Karin), van der Borden, D.M.R., Bremer, H.A. (Henk), Brons, J.T.J., Burggraaff, J.M. (Jan), Ceelie, H., Chon, H., Cikot, J.L.M., Delemarre, F.M.C., Diris, J.H.C., Doesburg-van Kleffens, M., van Dooren, I.M.A., van Duijnhoven, J.L.P., van Dunn, F.M., Duvekot, J.J. (Hans), Engbers, P., van Hulst, M.J.W., Feitsma, H., Fouraux, M.A., Franssen, MT, Frasa, M.A.M., van Gammeren, A.J., Gemund, N. (Nicolette) van, van der Graaf, F., Groot, C.J.M., Hackeng, C.M. (Christian), Ham, D.P. (David) van der, Hanssen, M., Hasaart, T.H.M. (Tom), Hendriks, H.A., Henskens, Y.M.C., Hermsen, B.B.J., Hogenboom, S., Hooker, A., Hudig, F, Huijssoon, A.G. (Annemarie), Huisjes, A.J.M. (Anjoke), Jonker, N., Kabel, P.J., van Kampen, C., de Keijzer, M.H., van de Kerkhof, D.H., Keuren, JFW, Kleiverda, G., Klinkspoor, J.H., Koehorst, S.G.A., Kok, M.O. (Maarten), Kok, R.D., Kok, J.B. (Jacques) de, Koops, A., Kortlandt, W. (Wouter), Langenveld, J. (J.), Leers, MPG, Leyte, A. (Anja), de Mare, A., Martens, G.D.M., Meekers, J.H., Meir, C.A. (Claudia) van, Metz, G.C.H. (Godfried), Michielse, E., Mostert, L.J., Bijvank, S., Oostenveld, E., Osmanovic, N., Oudijk, M.A. (Martijn), Mirani-Oostdijk, C.P., van Pampus, E. C. M., Papatsonis, D.N.M. (Dimitri), Peters, R.H.M., Ponjee, G.A.E. (Gabriëlle), Pontesilli, M., Porath, M. (Martina), Post, M.S., Pouwels, J.G.J., Prinzen, L., Roelofsen, J.M.T., Rondeel, J.J.M., Salm, P.C.M. (Paulien) van der, Scheepers, H.C.J. (Hubertina), Schippers, D.H. (Daniela), Schuitemaker, N.W.E. (Nico), Sikkema, J.M. (J. Marko), Slomp, J. (Jennita), Smit, J.W.A. (Jan), Snuif-de Lange, Y.S., van der Stappen, J.W.J., Steures, P. (Pieternel), Tax, G.H.M., Treskes, M., Ulenkate, H., van Unnik, G.A., van der Veen, B.S., Verhagen, T.E.M., Versendaal, J. (Johan), Visschers, B., Visser, O. (Oane), de Visser, H., De Vooght, KMK, de Vries, M.J., Waard, H. (Harm) de, Weerkamp, F. (Floor), Weinans, M.J.N. (Martin), de Wet, H., Wijnen, M. (Marit), Wijngaarden, W.J. (Wim) van, de Wit, A.C., Woiski, M.D. (Mallory), TeMp, O.H.S.G., Henriquez, D., Gillissen, A., Smith, S.M., Cramer, R.A., van den Akker, T., Zwart, J.J. (Joost), van Roosmalen, J.J., Bloemenkamp, KW, Bom, J.G., Adriaanse, H.J., van den Akker, E.S.A., Baas, M.I., Bank, C.M.C., Beek, E. van, de Boer, B.A.G., Boer, K. (Karin), van der Borden, D.M.R., Bremer, H.A. (Henk), Brons, J.T.J., Burggraaff, J.M. (Jan), Ceelie, H., Chon, H., Cikot, J.L.M., Delemarre, F.M.C., Diris, J.H.C., Doesburg-van Kleffens, M., van Dooren, I.M.A., van Duijnhoven, J.L.P., van Dunn, F.M., Duvekot, J.J. (Hans), Engbers, P., van Hulst, M.J.W., Feitsma, H., Fouraux, M.A., Franssen, MT, Frasa, M.A.M., van Gammeren, A.J., Gemund, N. (Nicolette) van, van der Graaf, F., Groot, C.J.M., Hackeng, C.M. (Christian), Ham, D.P. (David) van der, Hanssen, M., Hasaart, T.H.M. (Tom), Hendriks, H.A., Henskens, Y.M.C., Hermsen, B.B.J., Hogenboom, S., Hooker, A., Hudig, F, Huijssoon, A.G. (Annemarie), Huisjes, A.J.M. (Anjoke), Jonker, N., Kabel, P.J., van Kampen, C., de Keijzer, M.H., van de Kerkhof, D.H., Keuren, JFW, Kleiverda, G., Klinkspoor, J.H., Koehorst, S.G.A., Kok, M.O. (Maarten), Kok, R.D., Kok, J.B. (Jacques) de, Koops, A., Kortlandt, W. (Wouter), Langenveld, J. (J.), Leers, MPG, Leyte, A. (Anja), de Mare, A., Martens, G.D.M., Meekers, J.H., Meir, C.A. (Claudia) van, Metz, G.C.H. (Godfried), Michielse, E., Mostert, L.J., Bijvank, S., Oostenveld, E., Osmanovic, N., Oudijk, M.A. (Martijn), Mirani-Oostdijk, C.P., van Pampus, E. C. M., Papatsonis, D.N.M. (Dimitri), Peters, R.H.M., Ponjee, G.A.E. (Gabriëlle), Pontesilli, M., Porath, M. (Martina), Post, M.S., Pouwels, J.G.J., Prinzen, L., Roelofsen, J.M.T., Rondeel, J.J.M., Salm, P.C.M. (Paulien) van der, Scheepers, H.C.J. (Hubertina), Schippers, D.H. (Daniela), Schuitemaker, N.W.E. (Nico), Sikkema, J.M. (J. Marko), Slomp, J. (Jennita), Smit, J.W.A. (Jan), Snuif-de Lange, Y.S., van der Stappen, J.W.J., Steures, P. (Pieternel), Tax, G.H.M., Treskes, M., Ulenkate, H., van Unnik, G.A., van der Veen, B.S., Verhagen, T.E.M., Versendaal, J. (Johan), Visschers, B., Visser, O. (Oane), de Visser, H., De Vooght, KMK, de Vries, M.J., Waard, H. (Harm) de, Weerkamp, F. (Floor), Weinans, M.J.N. (Martin), de Wet, H., Wijnen, M. (Marit), Wijngaarden, W.J. (Wim) van, de Wit, A.C., Woiski, M.D. (Mallory), and TeMp, O.H.S.G.

Abstract

Background: The absence of a uniform and clinically relevant definition of severe postpartum haemorrhage hampers comparative studies and optimization of clinical management. The concept of persistent postpartum haemorrhage, based on refractoriness to initial first-line treatment, was proposed as an alternative to common definitions that are either based on estimations of blood loss or transfused units of packed red blood cells (RBC). We compared characteristics and outcomes of women with severe postpartum haemorrhage captured by these three types of definitions. Methods: In this large retrospective cohort study in 61 hospitals in the Netherlands we included 1391 consecutive women with postpartum haemorrhage who received either ≥4 units of RBC or a multicomponent transfusion. Clinical characteristics and outcomes of women with severe postpartum haemorrhage defined as persistent postpartum haemorrhage were compared to definitions based on estimated blood loss or transfused units of RBC within 24 h following birth. Adverse maternal outcome was a composite of maternal mortality, hysterectomy, arterial embolisation and intensive care unit admission. Results: One thousand two hundred sixty out of 1391 women (90.6%) with postpartum haemorrhage fulfilled the definition of persistent postpartum haemorrhage. The majority, 820/1260 (65.1%), fulfilled this definition within 1 h following birth, compared to 819/1391 (58.7%) applying the definition of ≥1 L blood loss and 37/845 (4.4%) applying the definition of ≥4 units of RBC. The definition persistent postpartum haemorrhage captured 430/471 adverse maternal outcomes (91.3%), compared to 471/471 (100%) for ≥1 L blood loss and 383/471 (81.3%) for ≥4 units of RBC. Persiste

Published
2019
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11. Clinical characteristics of women captured by extending the definition of severe postpartum haemorrhage with 'refractoriness to treatment': a cohort study

Author

Henriquez, D, Gillissen, A, Smith, SM, Cramer, RA, van den Akker, T, Zwart, JJ, van Roosmalen, JJ, Bloemenkamp, KW, Bom, JG, Adriaanse, HJ, Akker, ESA, Baas, MI, Bank, CMC, Beek, E, de Boer, BAG, Boer, K, van der Borden, DMR, Bremer, HA, Brons, JTJ, Burggraaff, JM, Ceelie, H, Chon, H, Cikot, JLM, Delemarre, FMC, Diris, JHC, Doesburg-van Kleffens, M, van Dooren, IMA, van Duijnhoven, JLP, van Dunn, FM, Duvekot, J.J., Engbers, P, Hulst, MJW, Feitsma, H, Fouraux, MA, Franssen, MT, Frasa, MAM, van Gammeren, AJ, Gemund, N, Graaf, F, Groot, CJM, Hackeng, CM, van der Ham, DP, Hanssen, M, Hasaart, THM, Hendriks, HA, Henskens, YMC, Hermsen, BBJ, Hogenboom, S, Hooker, A, Hudig, F, Huijssoon, AMG, Huisjes, AJM, Jonker, N, Kabel, PJ, van Kampen, C, de Keijzer, MH, van de Kerkhof, DH, Keuren, JFW, Kleiverda, G, Klinkspoor, JH, Koehorst, SGA, Kok, M, Kok, RD, de Kok, JB, Koops, A, Kortlandt, W, Langenveld, J, Leers, MPG, Leyte, A, de Mare, A, Martens, GDM, Meekers, JH, van Meir, CA, Metz, GCH, Michielse, E, Mostert, LJ, Bijvank, S, Oostenveld, E, Osmanovic, N, Oudijk, MA, Mirani-Oostdijk, CP, van Pampus, E C M, Papatsonis, DNM, Peters, RHM, Ponjee, GA, Pontesilli, M, Porath, MM, Post, MS, Pouwels, JGJ, Prinzen, L, Roelofsen, JMT, Rondeel, JJM, van der Salm, PCM, Scheepers, HCJ, Schippers, DH, Schuitemaker, NWE, Sikkema, JM, Slomp, J, Smit, JWA, Snuif-de Lange, YS, van der Stappen, JWJ, Steures, P, Tax, GHM, Treskes, M, Ulenkate, H, van Unnik, GA, van der Veen, BS, Verhagen, TEM, Versendaal, J, Visschers, B, Visser, O, Visser, H, De Vooght, KMK, Vries, MJ, Waard, H, Weerkamp, F, Weinans, MJN, de Wet, H, Wijnen, M (Mandy), van Wijngaarden, WJ, de Wit, AC, Woiski, MD, TeMp, OHSG, Henriquez, D, Gillissen, A, Smith, SM, Cramer, RA, van den Akker, T, Zwart, JJ, van Roosmalen, JJ, Bloemenkamp, KW, Bom, JG, Adriaanse, HJ, Akker, ESA, Baas, MI, Bank, CMC, Beek, E, de Boer, BAG, Boer, K, van der Borden, DMR, Bremer, HA, Brons, JTJ, Burggraaff, JM, Ceelie, H, Chon, H, Cikot, JLM, Delemarre, FMC, Diris, JHC, Doesburg-van Kleffens, M, van Dooren, IMA, van Duijnhoven, JLP, van Dunn, FM, Duvekot, J.J., Engbers, P, Hulst, MJW, Feitsma, H, Fouraux, MA, Franssen, MT, Frasa, MAM, van Gammeren, AJ, Gemund, N, Graaf, F, Groot, CJM, Hackeng, CM, van der Ham, DP, Hanssen, M, Hasaart, THM, Hendriks, HA, Henskens, YMC, Hermsen, BBJ, Hogenboom, S, Hooker, A, Hudig, F, Huijssoon, AMG, Huisjes, AJM, Jonker, N, Kabel, PJ, van Kampen, C, de Keijzer, MH, van de Kerkhof, DH, Keuren, JFW, Kleiverda, G, Klinkspoor, JH, Koehorst, SGA, Kok, M, Kok, RD, de Kok, JB, Koops, A, Kortlandt, W, Langenveld, J, Leers, MPG, Leyte, A, de Mare, A, Martens, GDM, Meekers, JH, van Meir, CA, Metz, GCH, Michielse, E, Mostert, LJ, Bijvank, S, Oostenveld, E, Osmanovic, N, Oudijk, MA, Mirani-Oostdijk, CP, van Pampus, E C M, Papatsonis, DNM, Peters, RHM, Ponjee, GA, Pontesilli, M, Porath, MM, Post, MS, Pouwels, JGJ, Prinzen, L, Roelofsen, JMT, Rondeel, JJM, van der Salm, PCM, Scheepers, HCJ, Schippers, DH, Schuitemaker, NWE, Sikkema, JM, Slomp, J, Smit, JWA, Snuif-de Lange, YS, van der Stappen, JWJ, Steures, P, Tax, GHM, Treskes, M, Ulenkate, H, van Unnik, GA, van der Veen, BS, Verhagen, TEM, Versendaal, J, Visschers, B, Visser, O, Visser, H, De Vooght, KMK, Vries, MJ, Waard, H, Weerkamp, F, Weinans, MJN, de Wet, H, Wijnen, M (Mandy), van Wijngaarden, WJ, de Wit, AC, Woiski, MD, and TeMp, OHSG

Published
2019

16. 3-D structural and functional characterization of the purified KATP channel complex Kir6.2-SUR1

Author

Mikhailov, MV, Campbell, JD, De Wet, H, Shimomura, K, Zadek, B, Collins, RF, Sansom, MS, Ford, RC, and Ashcroft, FM

Subjects
endocrine system
Abstract

ATP-sensitive potassium (K(ATP)) channels conduct potassium ions across cell membranes and thereby couple cellular energy metabolism to membrane electrical activity. Here, we report the heterologous expression and purification of a functionally active K(ATP) channel complex composed of pore-forming Kir6.2 and regulatory SUR1 subunits, and determination of its structure at 18 A resolution by single-particle electron microscopy. The purified channel shows ATP-ase activity similar to that of ATP-binding cassette proteins related to SUR1, and supports Rb(+) fluxes when reconstituted into liposomes. It has a compact structure, with four SUR1 subunits embracing a central Kir6.2 tetramer in both transmembrane and cytosolic domains. A cleft between adjacent SUR1s provides a route by which ATP may access its binding site on Kir6.2. The nucleotide-binding domains of adjacent SUR1 appear to interact, and form a large docking platform for cytosolic proteins. The structure, in combination with molecular modelling, suggests how SUR1 interacts with Kir6.2.

Published
2016

20. Medicinal Plants for Healing Sores and Wounds among the Communities Surrounding Ungoye Forest, Kwazulu-Natal, South Africa

Author

Mthethwa, N S and de Wet, H

Subjects
Traditional medicine, documentation, Ethno-survey, wounds
Abstract

The article is based on a study that aimed at documenting the ethno-knowledge on the usage of plants healing wounds and sores at the rural areas around uNgoye forest as well as document the methods of preparation and dosage forms of medicinal plants used by people around Ungoye forest. The survey was conducted in eighty homesteads. The information was collected through verbal communication and structured questionnaires. The focus was on the medicinal plants that grow in the Ungoye forest and around the homesteads. The survey revealed 33 plant species belonging to 27 families. The survey also revealed the one most commonly used plant for treating wounds and sores which is Hypericum aethiopicum (Unsukumbili). Out of the 33 plants species revealed 10 plant species were documented for the first time for the usage in wound and sore healing. The findings support the traditional value that the medicinal plants have in the primary healthcare system at uMgoye area, the need to put in place conservation measures to ensure the sustainable source and usage of medicinal plants and to encourage the domestication and cultivation of medicinal plants where possible.Keywords: Traditional medicine, documentation, Ethno-survey, wounds.

Published
2014

23. The ATPase activities of sulfonylurea receptor 2A and sulfonylurea receptor 2B are influenced by the C-terminal 42 amino acids

Author

De Wet, H, Fotinou, C, Amad, N, Dreger, M, and Ashcroft, F

Abstract

Unusually among ATP-binding cassette proteins, the sulfonylurea receptor (SUR) acts as a channel regulator. ATP-sensitive potassium channels are octameric complexes composed of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Two different genes encode SUR1 (ABCC8) and SUR2 (ABCC9), with the latter being differentially spliced to give SUR2A and SUR2B, which differ only in their C-terminal 42 amino acids. ATP-sensitive potassium channels containing these different SUR2 isoforms are differentially modulated by MgATP, with Kir6.2/SUR2B being activated more than Kir6.2/SUR2A. We show here that purified SUR2B has a lower ATPase activity and a 10-fold lower K m for MgATP than SUR2A. Similarly, the isolated nucleotide-binding domain (NBD) 2 of SUR2B was less active than that of SUR2A. We further found that the NBDs of SUR2B interact, and that the activity of full-length SUR cannot be predicted from that of either the isolated NBDs or NBD mixtures. Notably, deletion of the last 42 amino acids from NBD2 of SUR2 resulted in ATPase activity resembling that of NBD2 of SUR2A rather than that of NBD2 of SUR2B: this might indicate that these amino acids are responsible for the lower ATPase activity of SUR2B and the isolated NBD2 of SUR2B. We suggest that the lower ATPase activity of SUR2B may result in enhanced duration of the MgADP-bound state, leading to channel activation. © 2010 FEBS.

Published
2010

26. Studies of the ATPase activity of the ABC protein SUR1

Author

De Wet, H, Mikhailov, M, Fotinou, C, Dreger, M, Craig, T, Vénien-Bryan, C, and Ashcroft, F

Abstract

The ATP-sensitive potassium (K(ATP)) channel couples glucose metabolism to insulin secretion in pancreatic beta-cells. It comprises regulatory sulfonylurea receptor 1 and pore-forming Kir6.2 subunits. Binding and/or hydrolysis of Mg-nucleotides at the nucleotide-binding domains of sulfonylurea receptor 1 stimulates channel opening and leads to membrane hyperpolarization and inhibition of insulin secretion. We report here the first purification and functional characterization of sulfonylurea receptor 1. We also compared the ATPase activity of sulfonylurea receptor 1 with that of the isolated nucleotide-binding domains (fused to maltose-binding protein to improve solubility). Electron microscopy showed that nucleotide-binding domains purified as ring-like complexes corresponding to approximately 8 momomers. The ATPase activities expressed as maximal turnover rate [in nmol P(i).s(-1).(nmol protein)(-1)] were 0.03, 0.03, 0.13 and 0.08 for sulfonylurea receptor 1, nucleotide-binding domain 1, nucleotide-binding domain 2 and a mixture of nucleotide-binding domain 1 and nucleotide-binding domain 2, respectively. Corresponding K(m) values (in mm) were 0.1, 0.6, 0.65 and 0.56, respectively. Thus sulfonylurea receptor 1 has a lower K(m) than either of the isolated nucleotide-binding domains, and a lower maximal turnover rate than nucleotide-binding domain 2. Similar results were found with GTP, but the K(m) values were lower. Mutation of the Walker A lysine in nucleotide-binding domain 1 (K719A) or nucleotide-binding domain 2 (K1385M) inhibited the ATPase activity of sulfonylurea receptor 1 by 60% and 80%, respectively. Beryllium fluoride (K(i) 16 microm), but not MgADP, inhibited the ATPase activity of sulfonylurea receptor 1. In contrast, both MgADP and beryllium fluoride inhibited the ATPase activity of the nucleotide-binding domains. These data demonstrate that the ATPase activity of sulfonylurea receptor 1 differs from that of the isolated nucleotide-binding domains, suggesting that the transmembrane domains may influence the activity of the protein.

Published
2007

27. Gender differences in epidemiology and medical service utilisation among self-harm patients seeking treatment at an urban hospital in South Africa.

Author

Bantjes, J., Breet, E., De Wet, H., Khan, M., Weiss, R., and Lewis, I.

Abstract

Gender differences in patterns of self-harm in developed countries are well documented. Little is however known about gender differences in the epidemiology of self-harm in South Africa (SA) and about gender differences in medical service utilisation among self-harm patients. We set out to investigate gender differences in demographic, socio-cultural, clinical characteristics and medical service utilization of self-harm patients presenting at an urban hospital in SA. Demographic, socio-cultural, and clinical data were collected for 200 consecutive emergency room presentations of self-harm. Bivariate statistical and logistic regression analysis was employed to identify significant gender differences. Males constituted 40.5% of the sample. Male self-harm patients were more likely than women to have dependants, to injure themselves by hanging or laceration, to cite psychiatric illness as the reason for self-harm and to be admitted to an emergency psychiatric ward. Women self-harm patients were more likely than men to use prescription medications, cite family conflict as the precipitant of their self-harm, and to be treated in the emergency room and discharged. The proportion of males in the sample was higher than expected given what is known about gender differences in the prevalence of self-harm in SA. These findings draw attention to how contextual factors such as barriers to accessing health care may influence epidemiological self-harm data collected in hospital settings in low and middle income countries. Data also suggest that hospital based suicide prevention interventions may fail to reach women self-harm patients in SA who do not appear to access hospital care. [ABSTRACT FROM AUTHOR]

Published
2017

45. A novel mutation causing DEND syndrome

Author

Shimomura, K., primary, Hörster, F., additional, de Wet, H., additional, Flanagan, S. E., additional, Ellard, S., additional, Hattersley, A. T., additional, Wolf, N. I., additional, Ashcroft, F., additional, and Ebinger, F., additional

Published
2007
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46. ATPase and multidrug transport activities of the overexpressed yeast ABC protein Yor1p.

Author

UCL, Decottignies, Anabelle, Grant, A M, Nichols, J W, de Wet, H, McIntosh, D. B., Goffeau, André, UCL, Decottignies, Anabelle, Grant, A M, Nichols, J W, de Wet, H, McIntosh, D. B., and Goffeau, André

Abstract

The Saccharomyces cerevisiae genome encodes 15 full-size ATP binding cassette transporters (ABC), of which PDR5, SNQ2, and YOR1 are known to be regulated by the transcription factors Pdr1p and Pdr3p (pleiotropic drug resistance). We have identified two new ABC transporter-encoding genes, PDR10 and PDR15, which were up-regulated by the PDR1-3 mutation. These genes, as well as four other ABC transporter-encoding genes, were deleted in order to study the properties of Yor1p. The PDR1-3 gain-of-function mutant was then used to overproduce Yor1p up to 10% of the total plasma membrane proteins. Overexpressed Yor1p was photolabeled by [gamma-32P]2', 3'-O-(2,4,6-trinitrophenyl)-8-azido-ATP (K0.5 = 45 microM) and inhibited by ATP (KD = 0.3 mM) in plasma membranes. Solubilization and partial purification on sucrose gradient allowed to detect significant Yor1p ATP hydrolysis activity (approximately 100 nmol of Pi.min-1.mg-1). This activity was phospholipid-dependent and sensitive to low concentrations of vanadate (I50 = 0.3 microM) and oligomycin (I50 = 8.5 microg/ml). In vivo, we observed a correlation between the amount of Yor1p in the plasma membrane and the level of resistance to oligomycin. We also demonstrated that Yor1p drives an energy-dependent, proton uncoupler-insensitive, cellular extrusion of rhodamine B. Furthermore, cells lacking both Yor1p and Pdr5p (but not Snq2p) showed increased accumulation of the fluorescent derivative of 1-myristoyl-2-[6-(NBD)aminocaproyl]phosphatidylethanolamine. Despite their different topologies, both Yor1p and Pdr5p mediated the ATP-dependent translocation of similar drugs and phospholipids across the yeast cell membrane. Both ABC transporters exhibit ATP hydrolysis in vitro, but Pdr5p ATPase activity is about 15 times higher than that of Yor1p, which may indicate mechanistic or regulatory differences between the two enzymes.

Published
1998

50. Vegetative morphology and anatomy of Cissampelos in South Africa

Author

de Wet, H., Tilney, P.M., van Wyk, B.-E., and Botha, C.E.J.

Subjects
Cissampelos, Botany, Pulvinus, Morphology (biology), Leaf size, Plant Science, Biology, biology.organism_classification, Menispermaceae, Rhizome
Abstract

Representative samples of the four South African species of Cissampelos were collected for morphological and anatomical studies. Leaves and rhizomes of all four species are used in traditional medicine and any morphological and anatomical differences could be useful in forensic studies. Rhizomes of Cissampelos are easily identifiable because of the sieve-like appearance in transverse section of all members of the Menispermaceae, but C. hirta and C. mucronata are difficult to distinguish from one another. These two species are anatomically similar and morphologically distinguishable only by leaf texture, colour and the presence of a geniculate pulvinus in C. hirta. Furthermore, tanniniferous idioblasts occur in these two species but not in C. capensis and C. torulosa. Leaf size is important to distinguish C. capensis from the other three species and leaf shape to distinguish C. torulosa from the rest. C. capensis differs from the others in a number of anatomical features.

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