重瓣多花紫藤(豆科),一种中国新记录园艺植物

首次报道一种中国新记录园艺植物,重瓣多花紫藤[Wisteria floribunda(Willd.) DC. f. violaceo-plena(Schneider) Rehder & Wilson].     

五种攀缘植物光合作用与光因子关系的初步研究

城市垂直绿化常用的攀缘植物爬山虎、美国爬山虎、紫藤、常春藤、洋常春藤的净光合速率、呼吸速率、光能利用率及光补偿点等指标进行了测定和分析．结果表明,5种攀缘植物的净光合速率日变化显示出“双峰”。第一峰值出现在10：00～12：00,第二峰值出现在14：00～16：00,“午休”现象明显;呼吸速率的日变化也表现出“双峰”,第一峰值出现在11：00～13：00,第二峰值出现在14：00～17：00;常春藤、洋常春藤、爬山虎、美国爬山虎及紫藤的光补偿点分别为5．73、5．07、9．96、6．40和18．93μmol·m^-2·s^-1;紫藤在强光下的光能利用率较高,其次为美国爬山虎,而在弱光下洋常春藤光能利用率较高,可以认为,紫藤为典型的阳性植物,爬山虎、美国爬山虎为中性植物,常春藤、洋常春藤为阴性植物。     

不同土壤水分条件下紫藤叶片生理参数的光响应

测定了不同土壤湿度下2年生紫藤叶片光合速率（P_n）、蒸腾速率（T_r）及水分利用效率（WUE）等生理参数的光响应过程,探讨了紫藤正常生长发育所需的土壤水分和光照条件.结果表明:紫藤叶片的P_n、T_r及WUE对土壤湿度和光照强度的变化具有明显的阈值响应.维持紫藤正常生长（同时具有较高P_n和WUE）的土壤湿度范围为:体积含水量（W_v）15.3%～26.5%、相对含水量（W_r）46.4%～80.3%,最佳土壤湿度约为W_v 23.3%、W_r 70.6%.紫藤叶片对光照环境的适应性较强,在光合有效辐射强度（PAR）为600～1 600 μmol·m^-2·s^-1时,P_n和WUE具有较高水平,饱和光强在PAR为800～1 000 μmol·m^-2·s^-1.紫藤叶片光合作用非气孔限制的发生与土壤湿度与光照强度密切相关,W_v为18.4%～26.5%、W_r为55.8%～80.3%时,光合作用主要受气孔限制,光照强度的影响较小;超出此范围后,其受光照强度的影响较大,出现由气孔限制转变为非气孔限制的PAR临界值.紫藤正常生长允许的最低土壤湿度约为W_v 11.9%、W_r 36.1%,允许最高PAR约为1 000 μmol·m^-2·s^-1,是紫藤叶片光合机构受到破坏的临界点.     

山东临朐中中新世山旺组紫藤属(豆科)荚果化石的再观察

豆科紫藤属Wisteria约有5-6个现生种,间断分布于中国、日本和美国的温带地区,但化石记录表明,该属在新近纪可能广泛分布于捷克、荷兰、格鲁吉亚阿布哈兹、保加利亚、罗马尼亚、俄罗斯远东、日本和中国。因此,研究紫藤属化石有助于深入认识它的早期演化、分类、多样性、古生态和生物地理,其中荚果化石的分类价值和演化意义尤为显著。文中基于对产自山东临朐中中新世山旺组的山旺紫藤W.shanwangensis荚果化石的再观察,并结合紫藤属3个现生种——紫藤W.sinensis、藤萝W.villosa和多花紫藤W.floribunda的荚果发育特征,讨论这些化石的分类、演化、发育和埋藏学意义。结果进一步证明,山旺紫藤荚果化石与国产的2个现生种——紫藤和藤萝的荚果更为相似,呈倒披针形、种子较少和室间缢缩明显。比较而言,日本和美国产的紫藤属现生种——多花紫藤和美国紫藤W.frutescens的荚果呈线形、种子较多和室间缢缩不明显,而且日本中新世和上新世报道的紫藤属荚果化石与多花紫藤的荚果更为相似。然而,中国和日本报道的紫藤属荚果化石迄今都没发现被毛,这与现生种中最原始的美国紫藤的荚果相似,而与东亚紫藤属现生种密被绒毛的荚果形成显著差别。因此,中国、日本和美国的紫藤属种类可能早在中新世就已经发生了形态地理分化,而荚果无毛或许是该属演化过程中一个比较原始的性状;紫藤属现生种荚果在发育的中、后期果壁上具有与纵轴方向成锐角的倾斜纤维纹饰,它们在荚果完全成熟后导致果瓣沿缝线开裂并卷曲,卷曲的果瓣放入水中又能恢复平整。值得注意的是,山旺紫藤荚果化石果壁上也发现了类似的倾斜纤维纹饰,这表明它们在脱落保存时处在发育的中、后期,这一发育时期脱落的荚果更有可能保存为化石记录;山旺紫藤荚果化石果壁的碳质残片中还富含硅藻类,近似于远距直链藻Melosira distans和颗粒直链藻M.granulata这些浮游相的、生活在深水区的优势种。因此,山旺紫藤荚果脱离母体后可能沉积在湖水较深的地方,而且它也可能是在成熟开裂的状态下脱落,瓣片本来卷曲,被短程搬运至湖中,又在湖水的浸泡下恢复平整状态,而后经沉积物掩埋后形成化石。     

Bi-parental cytoplasmic DNA inheritance in Wisteria (Fabaceae): evidence from a natural experiment

Cytoplasmic inheritance was investigated in interspecific hybrids of Wisteria sinensis and W. floribunda. Species-specific nuclear, mitochondrial and plastid DNA markers were identified from wild-collected plants of each species in its native range. These markers provide evidence for the bi-parental transmission of plastids in hybrid swarms of these two species in the southeastern USA. These population level molecular data corroborate previous cytological evidence of this phenomenon in Wisteria.     

Large‐scale identification of secretome glycoproteins recognized by Wisteria floribunda agglutinin: A glycoproteomic approach to biomarker discovery

One of the promising approaches to the development of cancer diagnostic systems is quantification of a specific protein carrying cancerous glycans. Potential utility of Wisteria floribunda agglutinin (WFA) for such assays has been suggested for several cancer types. To develop such diagnostic systems, identification of WFA‐recognized glycoproteins is essential. Here, we successfully identified 504 WFA‐recognized glycoproteins from the secretome of HEK293T cells. Most of the identified proteins were likely soluble or single‐pass transmembrane proteins, which may serve as specific proteins for the diagnosis using biological fluids. Our method may help to discover marker glycoproteins for various cancers generating WFA‐recognized glycans.     

Use of Wisteria floribunda agglutinin affinity chromatography in the structural analysis of the bovine lactoferrin N-linked glycosylation

Background

Over the years, the N-glycosylation of both human and bovine lactoferrin (LF) has been studied extensively, however not all aspects have been studied in as much detail. Typically, the bovine LF complex-type N-glycans include certain epitopes, not found in human LF N-glycans, i.e. Gal(α1-3)Gal(β1-4)GlcNAc (αGal), GalNAc(β1-4)GlcNAc (LacdiNAc), and N-glycolylneuraminic acid (Neu5Gc). The combined presence of complex-type N-glycans, with αGal, LacdiNAc, LacNAc [Gal(β1-4)GlcNAc], Neu5Ac (N-acetylneuraminic acid), and Neu5Gc epitopes, and oligomannose-type N-glycans complicates the high-throughput analysis of such N-glycoprofiles highly.

Methods

For the structural analysis of enzymatically released N-glycan pools, containing both LacNAc and LacdiNAc epitopes, a prefractionation protocol based on Wisteria floribunda agglutinin affinity chromatography was developed. The sub pools were analysed by MALDI-TOF-MS and HPLC-FD profiling, including sequential exoglycosidase treatments.

Results

This protocol separates the N-glycan pool into three sub pools, with (1) free of LacdiNAc epitopes, (2) containing LacdiNAc epitopes, partially shielded by sialic acid, and (3) containing LacdiNAc epitopes, without shielding by sialic acid. Structural analysis by MALDI-TOF-MS and HPLC-FD showed a complex pattern of oligomannose-, hybrid-, and complex-type di-antennary structures, both with, and without LacdiNAc, αGal and sialic acid.

Conclusions

Applying the approach to bovine LF has led to a more detailed N-glycome pattern, including LacdiNAc, αGal, and Neu5Gc epitopes, than was shown in previous studies.

General significance

Bovine milk proteins contain glycosylation patterns that are absent in human milk proteins; particularly, the LacdiNAc epitope is abundant. Analysis of bovine milk serum proteins is therefore excessively complicated. The presented sub fractionation protocol allows a thorough analysis of the full scope of bovine milk protein glycosylation. This article is part of a Special Issue entitled Glycoproteomics.     

Wisteria floribunda agglutinin positive glycobiomarkers: a unique lectin as a serum biomarker probe in various diseases

Introduction: Serum proteins are generally glycosylated and solubilized, and are thus present as glycoproteins. The glycan structure of glycoproteins reflects cell differentiation status; glycan structures generated by diseased cells are distinguishable from those produced by healthy cells. Proteins may therefore serve as markers of tissues that secrete them. Several strategies for the identification of novel serum biomarkers using a combination of glycoscience-based technologies have been recently proposed. The selection of lectins for use as probes for identification of altered glycan structures represents a critical step.

Areas covered: This review describes the identification of Wisteria floribunda agglutinin (WFA) as a probe that recognizes the altered glycan structure of glycoproteins secreted by diseased cells. WFA may be employed as a probe for several diseases, e.g., liver fibrosis, liver cirrhosis, prostate cancer, ovarian cancer, and IgA nephropathy. The advantage of employing WFA as a serum biomarker probe is that only very small amounts of WFA-positive glycoproteins are present in serum; therefore, WFA background in serum is very low.

Expert commentary: Based on the findings to date, several WFA-positive serum biomarkers may be measured without pre-purification of target glycoproteins, indicating their utility as serum biomarkers in patients with various diseases.